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Database: PDB
Entry: 5HGJ
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HEADER    CELL ADHESION                           08-JAN-16   5HGJ              
TITLE     STRUCTURE OF INTEGRIN ALPHA1BETA1 AND ALPHA2BETA1 I-DOMAINS EXPLAIN   
TITLE    2 DIFFERENTIAL CALCIUM-MEDIATED LIGAND RECOGNITION                     
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: INTEGRIN ALPHA-1;                                          
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: EXTRACELLULAR VWFA DOMAIN RESIDUES 170-364;                
COMPND   5 SYNONYM: CD49 ANTIGEN-LIKE FAMILY MEMBER A,LAMININ AND COLLAGEN      
COMPND   6 RECEPTOR,VLA-1;                                                      
COMPND   7 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: ITGA1;                                                         
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    INTEGRIN, SIGNALING, ROSSMAN, I-DOMAIN, CELL ADHESION                 
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    K.L.BROWN,S.BANERJEE,A.FEIGLEY,H.ABE,T.BLACKWELL,R.ZENT,A.POZZI,      
AUTHOR   2 B.H.HUDSON                                                           
REVDAT   3   28-FEB-18 5HGJ    1       JRNL                                     
REVDAT   2   20-SEP-17 5HGJ    1       REMARK                                   
REVDAT   1   12-APR-17 5HGJ    0                                                
JRNL        AUTH   K.L.BROWN,S.BANERJEE,A.FEIGLEY,H.ABE,T.S.BLACKWELL,A.POZZI,  
JRNL        AUTH 2 B.G.HUDSON,R.ZENT                                            
JRNL        TITL   SALT-BRIDGE MODULATES DIFFERENTIAL CALCIUM-MEDIATED LIGAND   
JRNL        TITL 2 BINDING TO INTEGRIN ALPHA 1- AND ALPHA 2-I DOMAINS.          
JRNL        REF    SCI REP                       V.   8  2916 2018              
JRNL        REFN                   ESSN 2045-2322                               
JRNL        PMID   29440721                                                     
JRNL        DOI    10.1038/S41598-018-21231-1                                   
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.40 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (1.10_2155)                                   
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.40                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 47.98                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.380                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 93.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 66995                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.179                           
REMARK   3   R VALUE            (WORKING SET) : 0.178                           
REMARK   3   FREE R VALUE                     : 0.205                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 3349                            
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 48.0032 -  4.0358    0.93     2691   141  0.1595 0.1847        
REMARK   3     2  4.0358 -  3.2035    0.94     2687   142  0.1507 0.1601        
REMARK   3     3  3.2035 -  2.7986    0.96     2703   143  0.1742 0.1956        
REMARK   3     4  2.7986 -  2.5428    0.97     2740   144  0.1779 0.2122        
REMARK   3     5  2.5428 -  2.3605    0.96     2711   143  0.1802 0.2175        
REMARK   3     6  2.3605 -  2.2214    0.95     2681   141  0.1748 0.2170        
REMARK   3     7  2.2214 -  2.1101    0.96     2682   141  0.1795 0.2059        
REMARK   3     8  2.1101 -  2.0183    0.96     2719   144  0.1777 0.2193        
REMARK   3     9  2.0183 -  1.9406    0.96     2730   143  0.1786 0.1812        
REMARK   3    10  1.9406 -  1.8736    0.97     2702   143  0.1734 0.1957        
REMARK   3    11  1.8736 -  1.8150    0.92     2612   137  0.1789 0.2059        
REMARK   3    12  1.8150 -  1.7631    0.95     2678   141  0.1829 0.2306        
REMARK   3    13  1.7631 -  1.7167    0.97     2705   142  0.1829 0.2155        
REMARK   3    14  1.7167 -  1.6748    0.95     2697   141  0.1894 0.2165        
REMARK   3    15  1.6748 -  1.6367    0.97     2730   144  0.1874 0.2282        
REMARK   3    16  1.6367 -  1.6019    0.94     2657   140  0.1938 0.2225        
REMARK   3    17  1.6019 -  1.5699    0.96     2692   141  0.1904 0.2204        
REMARK   3    18  1.5699 -  1.5402    0.93     2618   138  0.2009 0.2330        
REMARK   3    19  1.5402 -  1.5127    0.94     2661   139  0.2038 0.2479        
REMARK   3    20  1.5127 -  1.4871    0.95     2656   140  0.2119 0.2466        
REMARK   3    21  1.4871 -  1.4631    0.93     2638   138  0.2351 0.2740        
REMARK   3    22  1.4631 -  1.4406    0.93     2591   137  0.2504 0.2996        
REMARK   3    23  1.4406 -  1.4194    0.90     2587   137  0.2623 0.2891        
REMARK   3    24  1.4194 -  1.3994    0.74     2078   109  0.2853 0.3135        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.160            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 20.850           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.006           3135                                  
REMARK   3   ANGLE     :  1.058           4241                                  
REMARK   3   CHIRALITY :  0.097            497                                  
REMARK   3   PLANARITY :  0.005            548                                  
REMARK   3   DIHEDRAL  : 20.041           1185                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 5HGJ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 11-JAN-16.                  
REMARK 100 THE DEPOSITION ID IS D_1000216977.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 04-DEC-15                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8                                  
REMARK 200  NUMBER OF CRYSTALS USED        : NULL                               
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 24-ID-C                            
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9791                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : PSI PILATUS 6M                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 67058                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.360                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 150.000                            
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 94.6                               
REMARK 200  DATA REDUNDANCY                : 3.600                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 14.7000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL                         
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 42.09                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.12                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 8000, TRIS-HCL, CALCIUM CHLORIDE,    
REMARK 280  SODIUM CHLORIDE, GLYCEROL, PH 8, VAPOR DIFFUSION, HANGING DROP,     
REMARK 280  TEMPERATURE 278K                                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y+1/2,-Z                                             
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000       47.97500            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
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 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B                                     
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. (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     ALA A   226                                                      
REMARK 465     GLU B   525                                                      
REMARK 465     ALA B   526                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     ALA B 523    O                                                   
REMARK 470     LEU B 524    CG   CD1  CD2                                       
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   OG   SER A   181     OE1  GLU A   183              1.58            
REMARK 500   NH2  ARG B   361     O    HOH B   701              1.85            
REMARK 500   O    GLY B   407     O    HOH B   702              1.94            
REMARK 500   NH1  ARG B   361     O    HOH B   703              1.97            
REMARK 500   O    VAL B   514     O    HOH B   703              1.98            
REMARK 500   ND2  ASN B   343     O    HOH B   704              2.01            
REMARK 500   NE2  GLN A    32     O    LYS A    67              2.02            
REMARK 500   OD1  ASN B   343     O    HOH B   705              2.08            
REMARK 500   OD1  ASP A    63     O    HOH A   701              2.13            
REMARK 500   O    HOH A   715     O    HOH B   737              2.15            
REMARK 500   OE1  GLU B   487     O    HOH B   706              2.16            
REMARK 500   O    HOH A   715     O    HOH A   752              2.17            
REMARK 500   O    HOH A   813     O    HOH A   880              2.17            
REMARK 500   OE1  GLU A    78     NH1  ARG A   108              2.18            
REMARK 500   O    HOH A   705     O    HOH A   880              2.18            
REMARK 500   O    HOH B   912     O    HOH B   915              2.18            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   O    HOH A   702     O    HOH A   902     1655     2.10            
REMARK 500   O    HOH A   724     O    HOH B   736     2546     2.12            
REMARK 500   NH2  ARG A   108     OD1  ASN B   379     2546     2.16            
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    GLU A  78   CA  -  CB  -  CG  ANGL. DEV. =  15.3 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    GLN A  68     -129.14   -127.99                                   
REMARK 500    MET A 111       67.20   -104.06                                   
REMARK 500    GLU A 122      -52.72   -120.36                                   
REMARK 500    GLN B 368     -130.48   -128.72                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH B 926        DISTANCE =  6.12 ANGSTROMS                       
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A 601  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 SER A  42   OG                                                     
REMARK 620 2 SER A  44   OG   89.6                                              
REMARK 620 3 ASP A 143   OD1  82.0  76.5                                        
REMARK 620 4 HOH A 748   O    72.5 150.1  77.4                                  
REMARK 620 5 HOH A 862   O    82.5  78.4 150.4 121.1                            
REMARK 620 6 HOH A 871   O   113.0 137.7 139.2  72.2  70.3                      
REMARK 620 7 HOH A 734   O   159.9  85.7  77.9 102.8 115.5  82.9                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA B 601  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 SER B 342   OG                                                     
REMARK 620 2 SER B 344   OG   93.5                                              
REMARK 620 3 ASP B 443   OD1  82.0  77.1                                        
REMARK 620 4 HOH B 735   O    72.6 150.5  75.3                                  
REMARK 620 5 HOH B 855   O    81.2  76.5 147.6 124.8                            
REMARK 620 6 HOH B 867   O   115.5 132.6 140.2  76.7  72.3                      
REMARK 620 7 HOH B 792   O   162.1  83.6  80.1 101.5 115.0  78.4                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA A 601                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 602                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 603                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA B 601                  
DBREF  5HGJ A   32   226  UNP    P56199   ITA1_HUMAN     170    364             
DBREF  5HGJ B  332   526  UNP    P56199   ITA1_HUMAN     170    364             
SEQRES   1 A  195  GLN LEU ASP ILE VAL ILE VAL LEU ASP GLY SER ASN SER          
SEQRES   2 A  195  ILE TYR PRO TRP ASP SER VAL THR ALA PHE LEU ASN ASP          
SEQRES   3 A  195  LEU LEU GLU ARG MET ASP ILE GLY PRO LYS GLN THR GLN          
SEQRES   4 A  195  VAL GLY ILE VAL GLN TYR GLY GLU ASN VAL THR HIS GLU          
SEQRES   5 A  195  PHE ASN LEU ASN LYS TYR SER SER THR GLU GLU VAL LEU          
SEQRES   6 A  195  VAL ALA ALA LYS LYS ILE VAL GLN ARG GLY GLY ARG GLN          
SEQRES   7 A  195  THR MET THR ALA LEU GLY ILE ASP THR ALA ARG LYS GLU          
SEQRES   8 A  195  ALA PHE THR GLU ALA ARG GLY ALA ARG ARG GLY VAL LYS          
SEQRES   9 A  195  LYS VAL MET VAL ILE VAL THR ASP GLY GLU SER HIS ASP          
SEQRES  10 A  195  ASN HIS ARG LEU LYS LYS VAL ILE GLN ASP CYS GLU ASP          
SEQRES  11 A  195  GLU ASN ILE GLN ARG PHE SER ILE ALA ILE LEU GLY SER          
SEQRES  12 A  195  TYR ASN ARG GLY ASN LEU SER THR GLU LYS PHE VAL GLU          
SEQRES  13 A  195  GLU ILE LYS SER ILE ALA SER GLU PRO THR GLU LYS HIS          
SEQRES  14 A  195  PHE PHE ASN VAL SER ASP GLU LEU ALA LEU VAL THR ILE          
SEQRES  15 A  195  VAL LYS THR LEU GLY GLU ARG ILE PHE ALA LEU GLU ALA          
SEQRES   1 B  195  GLN LEU ASP ILE VAL ILE VAL LEU ASP GLY SER ASN SER          
SEQRES   2 B  195  ILE TYR PRO TRP ASP SER VAL THR ALA PHE LEU ASN ASP          
SEQRES   3 B  195  LEU LEU GLU ARG MET ASP ILE GLY PRO LYS GLN THR GLN          
SEQRES   4 B  195  VAL GLY ILE VAL GLN TYR GLY GLU ASN VAL THR HIS GLU          
SEQRES   5 B  195  PHE ASN LEU ASN LYS TYR SER SER THR GLU GLU VAL LEU          
SEQRES   6 B  195  VAL ALA ALA LYS LYS ILE VAL GLN ARG GLY GLY ARG GLN          
SEQRES   7 B  195  THR MET THR ALA LEU GLY ILE ASP THR ALA ARG LYS GLU          
SEQRES   8 B  195  ALA PHE THR GLU ALA ARG GLY ALA ARG ARG GLY VAL LYS          
SEQRES   9 B  195  LYS VAL MET VAL ILE VAL THR ASP GLY GLU SER HIS ASP          
SEQRES  10 B  195  ASN HIS ARG LEU LYS LYS VAL ILE GLN ASP CYS GLU ASP          
SEQRES  11 B  195  GLU ASN ILE GLN ARG PHE SER ILE ALA ILE LEU GLY SER          
SEQRES  12 B  195  TYR ASN ARG GLY ASN LEU SER THR GLU LYS PHE VAL GLU          
SEQRES  13 B  195  GLU ILE LYS SER ILE ALA SER GLU PRO THR GLU LYS HIS          
SEQRES  14 B  195  PHE PHE ASN VAL SER ASP GLU LEU ALA LEU VAL THR ILE          
SEQRES  15 B  195  VAL LYS THR LEU GLY GLU ARG ILE PHE ALA LEU GLU ALA          
HET     CA  A 601       1                                                       
HET     CL  A 602       1                                                       
HET    GOL  A 603       6                                                       
HET     CA  B 601       1                                                       
HETNAM      CA CALCIUM ION                                                      
HETNAM      CL CHLORIDE ION                                                     
HETNAM     GOL GLYCEROL                                                         
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   3   CA    2(CA 2+)                                                     
FORMUL   4   CL    CL 1-                                                        
FORMUL   5  GOL    C3 H8 O3                                                     
FORMUL   7  HOH   *460(H2 O)                                                    
HELIX    1 AA1 TRP A   48  GLU A   60  1                                  13    
HELIX    2 AA2 SER A   91  LYS A  101  1                                  11    
HELIX    3 AA3 MET A  111  GLU A  122  1                                  12    
HELIX    4 AA4 THR A  125  GLY A  129  5                                   5    
HELIX    5 AA5 ASP A  148  HIS A  150  5                                   3    
HELIX    6 AA6 ARG A  151  GLU A  162  1                                  12    
HELIX    7 AA7 LEU A  172  GLY A  178  1                                   7    
HELIX    8 AA8 THR A  182  ALA A  193  1                                  12    
HELIX    9 AA9 PRO A  196  HIS A  200  1                                   5    
HELIX   10 AB1 ASP A  206  THR A  212  5                                   7    
HELIX   11 AB2 ILE A  213  PHE A  222  1                                  10    
HELIX   12 AB3 TRP B  348  GLU B  360  1                                  13    
HELIX   13 AB4 SER B  391  LYS B  401  1                                  11    
HELIX   14 AB5 MET B  411  GLU B  422  1                                  12    
HELIX   15 AB6 THR B  425  GLY B  429  5                                   5    
HELIX   16 AB7 ASP B  448  HIS B  450  5                                   3    
HELIX   17 AB8 ARG B  451  GLU B  462  1                                  12    
HELIX   18 AB9 LEU B  472  GLY B  478  1                                   7    
HELIX   19 AC1 THR B  482  ALA B  493  1                                  12    
HELIX   20 AC2 PRO B  496  HIS B  500  1                                   5    
HELIX   21 AC3 ASP B  506  THR B  512  5                                   7    
HELIX   22 AC4 ILE B  513  ALA B  523  1                                  11    
SHEET    1 AA1 6 VAL A  80  PHE A  84  0                                        
SHEET    2 AA1 6 GLN A  70  TYR A  76 -1  N  GLN A  75   O  THR A  81           
SHEET    3 AA1 6 LEU A  33  ASP A  40  1  N  ILE A  37   O  VAL A  74           
SHEET    4 AA1 6 LYS A 135  THR A 142  1  O  VAL A 139   N  VAL A  38           
SHEET    5 AA1 6 ILE A 164  ILE A 171  1  O  PHE A 167   N  MET A 138           
SHEET    6 AA1 6 PHE A 201  VAL A 204  1  O  VAL A 204   N  ALA A 170           
SHEET    1 AA2 6 VAL B 380  PHE B 384  0                                        
SHEET    2 AA2 6 GLN B 370  TYR B 376 -1  N  GLN B 375   O  THR B 381           
SHEET    3 AA2 6 LEU B 333  ASP B 340  1  N  ILE B 335   O  GLN B 370           
SHEET    4 AA2 6 LYS B 435  THR B 442  1  O  VAL B 439   N  VAL B 338           
SHEET    5 AA2 6 ILE B 464  ILE B 471  1  O  GLN B 465   N  MET B 438           
SHEET    6 AA2 6 PHE B 501  VAL B 504  1  O  VAL B 504   N  ALA B 470           
LINK         OG  SER A  42                CA    CA A 601     1555   1555  2.74  
LINK         OG  SER A  44                CA    CA A 601     1555   1555  2.32  
LINK         OD1 ASP A 143                CA    CA A 601     1555   1555  2.40  
LINK         OG  SER B 342                CA    CA B 601     1555   1555  2.59  
LINK         OG  SER B 344                CA    CA B 601     1555   1555  2.37  
LINK         OD1 ASP B 443                CA    CA B 601     1555   1555  2.38  
LINK        CA    CA A 601                 O   HOH A 748     1555   1555  2.33  
LINK        CA    CA A 601                 O   HOH A 862     1555   1555  2.45  
LINK        CA    CA A 601                 O   HOH A 871     1555   1555  2.47  
LINK        CA    CA A 601                 O   HOH A 734     1555   1555  2.44  
LINK        CA    CA B 601                 O   HOH B 735     1555   1555  2.31  
LINK        CA    CA B 601                 O   HOH B 855     1555   1555  2.54  
LINK        CA    CA B 601                 O   HOH B 867     1555   1555  2.42  
LINK        CA    CA B 601                 O   HOH B 792     1555   1555  2.35  
CISPEP   1 TYR A   46    PRO A   47          0        -6.25                     
CISPEP   2 GLU A  195    PRO A  196          0        -2.39                     
CISPEP   3 TYR B  346    PRO B  347          0        -6.15                     
CISPEP   4 GLU B  495    PRO B  496          0        -1.34                     
SITE     1 AC1  7 SER A  42  SER A  44  ASP A 143  HOH A 734                    
SITE     2 AC1  7 HOH A 748  HOH A 862  HOH A 871                               
SITE     1 AC2  1 THR A 216                                                     
SITE     1 AC3  3 GLU A 122  HOH A 747  HOH A 809                               
SITE     1 AC4  7 SER B 342  SER B 344  ASP B 443  HOH B 735                    
SITE     2 AC4  7 HOH B 792  HOH B 855  HOH B 867                               
CRYST1   37.369   95.950   53.078  90.00 104.00  90.00 P 1 21 1      4          
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      0.026760  0.000000  0.006670        0.00000                         
SCALE2      0.000000  0.010422  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.019417        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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