Tree Display

AceDB Schema

XML Display

Feedback

LongText Report for: 5h3b-pdb

Name Class
5h3b-pdb
HEADER    HYDROLASE                               21-OCT-16   5H3B              
TITLE     CRYSTAL STRUCTURE OF SEMET-BIOG FROM HAEMOPHILUS INFLUENZAE AT 1.49   
TITLE    2 ANGSTROMS RESOLUTION                                                 
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: UNCHARACTERIZED PROTEIN HI_1552;                           
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 EC: 3.1.1.1;                                                         
COMPND   5 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HAEMOPHILUS INFLUENZAE RD KW20;                 
SOURCE   3 ORGANISM_TAXID: 71421;                                               
SOURCE   4 STRAIN: KW20;                                                        
SOURCE   5 GENE: HI_1552;                                                       
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21;                            
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 511693;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21;                                      
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID                               
KEYWDS    ALPHA/BETA-HYDROLASE FOLD, PIMELOYL-ACP METHYL ESTERASE, BIOTIN       
KEYWDS   2 BIOSYNTHESIS, HYDROLASE                                              
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.SHI,Z.GUO                                                           
REVDAT   1   07-DEC-16 5H3B    0                                                
JRNL        AUTH   J.SHI,X.CAO,Y.CHEN,J.E.CRONAN,Z.GUO                          
JRNL        TITL   AN ATYPICAL ALPHA/BETA HYDROLASE FOLD REVEALED IN THE        
JRNL        TITL 2 CRYSTAL STRUCTURE OF PIMELOYL-ACYL CARRIER PROTEIN METHYL    
JRNL        TITL 3 ESTERASE BIOG FROM HAEMOPHILUS INFLUENZAE                    
JRNL        REF    BIOCHEMISTRY                               2016              
JRNL        REFN                   ISSN 0006-2960                               
JRNL        DOI    10.1021/ACS.BIOCHEM.6B00818                                  
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.49 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX 1.8.4_1496                                    
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 : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.49                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 32.45                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 97.4                           
REMARK   3   NUMBER OF REFLECTIONS             : 68819                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.148                           
REMARK   3   R VALUE            (WORKING SET) : 0.147                           
REMARK   3   FREE R VALUE                     : 0.182                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 2.840                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1954                            
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 32.4577 -  3.5945    1.00     4995   144  0.1439 0.1606        
REMARK   3     2  3.5945 -  2.8536    1.00     4936   144  0.1485 0.1794        
REMARK   3     3  2.8536 -  2.4930    1.00     4892   152  0.1544 0.1588        
REMARK   3     4  2.4930 -  2.2652    1.00     4929   133  0.1366 0.1927        
REMARK   3     5  2.2652 -  2.1028    1.00     4861   141  0.1277 0.1569        
REMARK   3     6  2.1028 -  1.9789    0.99     4909   145  0.1280 0.1763        
REMARK   3     7  1.9789 -  1.8798    0.99     4807   146  0.1256 0.1713        
REMARK   3     8  1.8798 -  1.7980    0.98     4782   138  0.1394 0.1974        
REMARK   3     9  1.7980 -  1.7288    0.98     4795   151  0.1455 0.2058        
REMARK   3    10  1.7288 -  1.6691    0.97     4767   124  0.1569 0.1955        
REMARK   3    11  1.6691 -  1.6169    0.96     4675   151  0.1671 0.2292        
REMARK   3    12  1.6169 -  1.5707    0.96     4665   134  0.1778 0.2690        
REMARK   3    13  1.5707 -  1.5293    0.94     4607   129  0.2054 0.2594        
REMARK   3    14  1.5293 -  1.4920    0.87     4245   122  0.2297 0.3163        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : NULL                                          
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)     : 0.150            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 19.760           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 25.32                          
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      :  0.007           3636                                  
REMARK   3   ANGLE     :  1.126           4954                                  
REMARK   3   CHIRALITY :  0.044            523                                  
REMARK   3   PLANARITY :  0.005            630                                  
REMARK   3   DIHEDRAL  : 13.427           1277                                  
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 5H3B COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 27-OCT-16.                  
REMARK 100 THE DEPOSITION ID IS D_1300001937.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 25-DEC-15                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 5.6                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SSRF                               
REMARK 200  BEAMLINE                       : BL17U                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9792                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315R                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000, HKL                      
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000, HKL                      
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 70407                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.490                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 32.450                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.6                               
REMARK 200  DATA REDUNDANCY                : 7.400                              
REMARK 200  R MERGE                    (I) : 0.08200                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 10.9000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.49                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.54                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 96.4                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 6.50                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.69000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD                          
REMARK 200 SOFTWARE USED: PHENIX 1.8.4_1496                                     
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 43.73                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.19                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 10%(V/V) ISO-PROPANOL, 0.1M CITRIC       
REMARK 280  ACID/SODIUM CITRATE PH 5.6, 22% PEG 4000, VAPOR DIFFUSION,          
REMARK 280  HANGING DROP, TEMPERATURE 289K                                      
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       34.73550            
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 TOTAL BURIED SURFACE AREA: 240 ANGSTROM**2                           
REMARK 350 SURFACE AREA OF THE COMPLEX: 9420 ANGSTROM**2                        
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -1.0 KCAL/MOL                         
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 TOTAL BURIED SURFACE AREA: 0 ANGSTROM**2                             
REMARK 350 SURFACE AREA OF THE COMPLEX: 9300 ANGSTROM**2                        
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 0.0 KCAL/MOL                          
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     HIS A   215                                                      
REMARK 465     LEU A   216                                                      
REMARK 465     GLU A   217                                                      
REMARK 465     HIS A   218                                                      
REMARK 465     HIS A   219                                                      
REMARK 465     HIS A   220                                                      
REMARK 465     HIS A   221                                                      
REMARK 465     HIS A   222                                                      
REMARK 465     HIS A   223                                                      
REMARK 465     HIS B   215                                                      
REMARK 465     LEU B   216                                                      
REMARK 465     GLU B   217                                                      
REMARK 465     HIS B   218                                                      
REMARK 465     HIS B   219                                                      
REMARK 465     HIS B   220                                                      
REMARK 465     HIS B   221                                                      
REMARK 465     HIS B   222                                                      
REMARK 465     HIS B   223                                                      
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     GLU A  34    CG   CD   OE1  OE2                                  
REMARK 470     ARG A  79    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLN A 146    OE1                                                 
REMARK 470     GLU A 195    CD   OE1  OE2                                       
REMARK 470     ASP A 214    OD1  OD2                                            
REMARK 470     LYS B   2    NZ                                                  
REMARK 470     LYS B   4    CE   NZ                                             
REMARK 470     TYR B   8    CD1  CD2  CE1  CE2  CZ   OH                         
REMARK 470     GLN B   9    OE1  NE2                                            
REMARK 470     ASN B  28    OD1                                                 
REMARK 470     GLU B  34    CB   CG   CD   OE1  OE2                             
REMARK 470     ASN B  48    CG   OD1  ND2                                       
REMARK 470     ASP B  50    CG   OD1  OD2                                       
REMARK 470     ARG B  57    CG   CD                                             
REMARK 470     ILE B  78    CD1                                                 
REMARK 470     ARG B  79    CD   NE   CZ   NH1  NH2                             
REMARK 470     GLU B 113    CG   CD   OE1  OE2                                  
REMARK 470     ASN B 114    CG   OD1  ND2                                       
REMARK 470     ARG B 116    CG   CD                                             
REMARK 470     LYS B 118    CG   CD   CE   NZ                                   
REMARK 470     LYS B 127    CG   CD   CE   NZ                                   
REMARK 470     ASP B 142    CB   CG   OD1  OD2                                  
REMARK 470     GLN B 146    CD   OE1  NE2                                       
REMARK 470     GLU B 197    OE1  OE2                                            
REMARK 470     ASP B 214    O    OD1  OD2                                       
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   O    HOH A   441     O    HOH A   621              1.48            
REMARK 500   O    HOH A   453     O    HOH A   626              1.55            
REMARK 500   O    HOH B   326     O    HOH B   409              1.59            
REMARK 500   O    HOH A   415     O    HOH A   647              1.68            
REMARK 500   O    HOH A   693     O    HOH A   725              1.75            
REMARK 500   O    HOH B   339     O    HOH B   417              1.76            
REMARK 500   O    HOH A   676     O    HOH A   732              1.82            
REMARK 500   O    HOH A   567     O    HOH A   654              1.83            
REMARK 500   O    HOH A   659     O    HOH A   728              1.99            
REMARK 500   O    HOH A   626     O    HOH A   665              2.00            
REMARK 500   O    HOH A   403     O    HOH A   625              2.01            
REMARK 500   O    HOH A   641     O    HOH A   647              2.01            
REMARK 500   O    HOH A   559     O    HOH A   651              2.02            
REMARK 500   O    HOH A   425     O    HOH A   508              2.03            
REMARK 500   O    HOH A   402     O    HOH A   645              2.03            
REMARK 500   O    HOH B   362     O    HOH B   419              2.04            
REMARK 500   O    HOH A   561     O    HOH A   661              2.09            
REMARK 500   O    HOH A   555     O    HOH A   684              2.10            
REMARK 500   O    HOH A   662     O    HOH A   668              2.11            
REMARK 500   O    HOH A   473     O    HOH A   619              2.11            
REMARK 500   O    HOH B   412     O    HOH B   432              2.14            
REMARK 500   O    HOH A   462     O    HOH A   699              2.14            
REMARK 500   O    HOH A   695     O    HOH B   417              2.16            
REMARK 500   O    HOH A   653     O    HOH A   693              2.18            
REMARK 500   O    HOH A   540     O    HOH A   600              2.19            
REMARK 500   O    HOH A   441     O    HOH A   549              2.19            
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   455     O    HOH A   615     1655     1.71            
REMARK 500   O    HOH A   447     O    HOH A   504     2546     1.75            
REMARK 500   O    HOH A   621     O    HOH A   651     1655     1.93            
REMARK 500   O    HOH A   559     O    HOH A   621     1455     1.94            
REMARK 500   O    HOH A   441     O    HOH A   651     1655     2.11            
REMARK 500   O    HOH A   723     O    HOH A   730     1655     2.13            
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    ARG A  57      -77.12    -80.43                                   
REMARK 500    SER A  65     -128.34     63.53                                   
REMARK 500    SER B  65     -129.76     63.80                                   
REMARK 500    ILE B 177      -65.18   -104.32                                   
REMARK 500    LEU B 189       -2.40     70.98                                   
REMARK 500    ARG B 190      -80.14   -100.65                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 301                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue IPA A 302                 
DBREF  5H3B A    1   215  UNP    P44251   Y1552_HAEIN      1    215             
DBREF  5H3B B    1   215  UNP    P44251   Y1552_HAEIN      1    215             
SEQADV 5H3B LEU A  216  UNP  P44251              EXPRESSION TAG                 
SEQADV 5H3B GLU A  217  UNP  P44251              EXPRESSION TAG                 
SEQADV 5H3B HIS A  218  UNP  P44251              EXPRESSION TAG                 
SEQADV 5H3B HIS A  219  UNP  P44251              EXPRESSION TAG                 
SEQADV 5H3B HIS A  220  UNP  P44251              EXPRESSION TAG                 
SEQADV 5H3B HIS A  221  UNP  P44251              EXPRESSION TAG                 
SEQADV 5H3B HIS A  222  UNP  P44251              EXPRESSION TAG                 
SEQADV 5H3B HIS A  223  UNP  P44251              EXPRESSION TAG                 
SEQADV 5H3B LEU B  216  UNP  P44251              EXPRESSION TAG                 
SEQADV 5H3B GLU B  217  UNP  P44251              EXPRESSION TAG                 
SEQADV 5H3B HIS B  218  UNP  P44251              EXPRESSION TAG                 
SEQADV 5H3B HIS B  219  UNP  P44251              EXPRESSION TAG                 
SEQADV 5H3B HIS B  220  UNP  P44251              EXPRESSION TAG                 
SEQADV 5H3B HIS B  221  UNP  P44251              EXPRESSION TAG                 
SEQADV 5H3B HIS B  222  UNP  P44251              EXPRESSION TAG                 
SEQADV 5H3B HIS B  223  UNP  P44251              EXPRESSION TAG                 
SEQRES   1 A  223  MSE LYS THR LYS PHE TYR ASP TYR GLN GLY GLU HIS LEU          
SEQRES   2 A  223  ILE LEU TYR PHE ALA GLY TRP GLY THR PRO PRO ASP ALA          
SEQRES   3 A  223  VAL ASN HIS LEU ILE LEU PRO GLU ASN HIS ASP LEU LEU          
SEQRES   4 A  223  ILE CYS TYR ASP TYR GLN ASP LEU ASN LEU ASP PHE ASP          
SEQRES   5 A  223  LEU SER ALA TYR ARG HIS ILE ARG LEU VAL ALA TRP SER          
SEQRES   6 A  223  MSE GLY VAL TRP VAL ALA GLU ARG VAL LEU GLN GLY ILE          
SEQRES   7 A  223  ARG LEU LYS SER ALA THR ALA VAL ASN GLY THR GLY LEU          
SEQRES   8 A  223  PRO CYS ASP ASP SER PHE GLY ILE PRO TYR ALA ILE PHE          
SEQRES   9 A  223  LYS GLY THR LEU GLU ASN LEU THR GLU ASN THR ARG LEU          
SEQRES  10 A  223  LYS PHE GLU ARG ARG ILE CYS GLY ASP LYS ALA SER PHE          
SEQRES  11 A  223  GLU ARG TYR GLN LEU PHE PRO ALA ARG PRO PHE ASP GLU          
SEQRES  12 A  223  ILE HIS GLN GLU LEU THR ALA LEU PHE ALA MSE ILE GLN          
SEQRES  13 A  223  GLN ASP LYS ARG ILE ASP LEU ILE HIS TRP ALA ASN ALA          
SEQRES  14 A  223  TRP VAL SER SER ARG ASP LYS ILE PHE THR PRO ALA ASN          
SEQRES  15 A  223  GLN HIS GLN TYR TRP ALA LEU ARG CYS ALA VAL GLN GLU          
SEQRES  16 A  223  ILE GLU GLY GLU HIS TYR VAL PHE SER ARG PHE THR HIS          
SEQRES  17 A  223  TRP SER ALA LEU TRP ASP HIS LEU GLU HIS HIS HIS HIS          
SEQRES  18 A  223  HIS HIS                                                      
SEQRES   1 B  223  MSE LYS THR LYS PHE TYR ASP TYR GLN GLY GLU HIS LEU          
SEQRES   2 B  223  ILE LEU TYR PHE ALA GLY TRP GLY THR PRO PRO ASP ALA          
SEQRES   3 B  223  VAL ASN HIS LEU ILE LEU PRO GLU ASN HIS ASP LEU LEU          
SEQRES   4 B  223  ILE CYS TYR ASP TYR GLN ASP LEU ASN LEU ASP PHE ASP          
SEQRES   5 B  223  LEU SER ALA TYR ARG HIS ILE ARG LEU VAL ALA TRP SER          
SEQRES   6 B  223  MSE GLY VAL TRP VAL ALA GLU ARG VAL LEU GLN GLY ILE          
SEQRES   7 B  223  ARG LEU LYS SER ALA THR ALA VAL ASN GLY THR GLY LEU          
SEQRES   8 B  223  PRO CYS ASP ASP SER PHE GLY ILE PRO TYR ALA ILE PHE          
SEQRES   9 B  223  LYS GLY THR LEU GLU ASN LEU THR GLU ASN THR ARG LEU          
SEQRES  10 B  223  LYS PHE GLU ARG ARG ILE CYS GLY ASP LYS ALA SER PHE          
SEQRES  11 B  223  GLU ARG TYR GLN LEU PHE PRO ALA ARG PRO PHE ASP GLU          
SEQRES  12 B  223  ILE HIS GLN GLU LEU THR ALA LEU PHE ALA MSE ILE GLN          
SEQRES  13 B  223  GLN ASP LYS ARG ILE ASP LEU ILE HIS TRP ALA ASN ALA          
SEQRES  14 B  223  TRP VAL SER SER ARG ASP LYS ILE PHE THR PRO ALA ASN          
SEQRES  15 B  223  GLN HIS GLN TYR TRP ALA LEU ARG CYS ALA VAL GLN GLU          
SEQRES  16 B  223  ILE GLU GLY GLU HIS TYR VAL PHE SER ARG PHE THR HIS          
SEQRES  17 B  223  TRP SER ALA LEU TRP ASP HIS LEU GLU HIS HIS HIS HIS          
SEQRES  18 B  223  HIS HIS                                                      
MODRES 5H3B MSE A    1  MET  MODIFIED RESIDUE                                   
MODRES 5H3B MSE A   66  MET  MODIFIED RESIDUE                                   
MODRES 5H3B MSE A  154  MET  MODIFIED RESIDUE                                   
MODRES 5H3B MSE B    1  MET  MODIFIED RESIDUE                                   
MODRES 5H3B MSE B   66  MET  MODIFIED RESIDUE                                   
MODRES 5H3B MSE B  154  MET  MODIFIED RESIDUE                                   
HET    MSE  A   1       8                                                       
HET    MSE  A  66       8                                                       
HET    MSE  A 154      13                                                       
HET    MSE  B   1      13                                                       
HET    MSE  B  66      13                                                       
HET    MSE  B 154      13                                                       
HET    GOL  A 301       6                                                       
HET    IPA  A 302       4                                                       
HETNAM     MSE SELENOMETHIONINE                                                 
HETNAM     GOL GLYCEROL                                                         
HETNAM     IPA ISOPROPYL ALCOHOL                                                
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
HETSYN     IPA 2-PROPANOL                                                       
FORMUL   1  MSE    6(C5 H11 N O2 SE)                                            
FORMUL   3  GOL    C3 H8 O3                                                     
FORMUL   4  IPA    C3 H8 O                                                      
FORMUL   5  HOH   *470(H2 O)                                                    
HELIX    1 AA1 PRO A   23  ASN A   28  5                                   6    
HELIX    2 AA2 MSE A   66  LEU A   75  1                                  10    
HELIX    3 AA3 PRO A  100  ASN A  110  1                                  11    
HELIX    4 AA4 THR A  112  GLY A  125  1                                  14    
HELIX    5 AA5 ASP A  126  GLN A  134  1                                   9    
HELIX    6 AA6 PRO A  140  ASP A  158  1                                  19    
HELIX    7 AA7 THR A  179  ALA A  188  1                                  10    
HELIX    8 AA8 VAL A  202  PHE A  206  5                                   5    
HELIX    9 AA9 HIS A  208  TRP A  213  5                                   6    
HELIX   10 AB1 PRO B   23  ASN B   28  5                                   6    
HELIX   11 AB2 ASP B   52  TYR B   56  5                                   5    
HELIX   12 AB3 MSE B   66  LEU B   75  1                                  10    
HELIX   13 AB4 PRO B  100  ASN B  110  1                                  11    
HELIX   14 AB5 THR B  112  GLY B  125  1                                  14    
HELIX   15 AB6 ASP B  126  GLN B  134  1                                   9    
HELIX   16 AB7 PRO B  140  ASP B  158  1                                  19    
HELIX   17 AB8 THR B  179  ALA B  188  1                                  10    
HELIX   18 AB9 VAL B  202  PHE B  206  5                                   5    
HELIX   19 AC1 HIS B  208  ASP B  214  1                                   7    
SHEET    1 AA1 7 LYS A   2  TYR A   6  0                                        
SHEET    2 AA1 7 HIS A  36  TYR A  42 -1  O  LEU A  38   N  TYR A   6           
SHEET    3 AA1 7 HIS A  12  PHE A  17  1  N  TYR A  16   O  CYS A  41           
SHEET    4 AA1 7 ILE A  59  TRP A  64  1  O  ARG A  60   N  LEU A  15           
SHEET    5 AA1 7 SER A  82  VAL A  86  1  O  VAL A  86   N  ALA A  63           
SHEET    6 AA1 7 ASN A 168  SER A 172  1  O  TRP A 170   N  ALA A  85           
SHEET    7 AA1 7 ALA A 192  ILE A 196  1  O  GLN A 194   N  ALA A 169           
SHEET    1 AA2 7 LYS B   2  TYR B   6  0                                        
SHEET    2 AA2 7 HIS B  36  TYR B  42 -1  O  LEU B  38   N  TYR B   6           
SHEET    3 AA2 7 HIS B  12  PHE B  17  1  N  TYR B  16   O  CYS B  41           
SHEET    4 AA2 7 ILE B  59  TRP B  64  1  O  ARG B  60   N  LEU B  15           
SHEET    5 AA2 7 SER B  82  VAL B  86  1  O  SER B  82   N  LEU B  61           
SHEET    6 AA2 7 ASN B 168  SER B 172  1  O  TRP B 170   N  ALA B  85           
SHEET    7 AA2 7 ALA B 192  ILE B 196  1  O  GLN B 194   N  ALA B 169           
LINK         C   MSE A   1                 N   LYS A   2     1555   1555  1.33  
LINK         C   SER A  65                 N   MSE A  66     1555   1555  1.31  
LINK         C   MSE A  66                 N   GLY A  67     1555   1555  1.31  
LINK         C   ALA A 153                 N   MSE A 154     1555   1555  1.33  
LINK         C   MSE A 154                 N   ILE A 155     1555   1555  1.34  
LINK         C   MSE B   1                 N   LYS B   2     1555   1555  1.33  
LINK         C   SER B  65                 N   MSE B  66     1555   1555  1.33  
LINK         C   MSE B  66                 N   GLY B  67     1555   1555  1.33  
LINK         C   ALA B 153                 N   MSE B 154     1555   1555  1.33  
LINK         C   MSE B 154                 N   ILE B 155     1555   1555  1.33  
SITE     1 AC1  8 TYR A   6  TYR A   8  ASN A  28  LEU A  30                    
SITE     2 AC1  8 LEU A  32  HOH A 425  HOH A 442  HOH A 514                    
SITE     1 AC2  4 GLY A  19  TRP A  20  THR A  22  SER A  65                    
CRYST1   44.154   69.471   72.034  90.00  93.15  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      0.022648  0.000000  0.001247        0.00000                         
SCALE2      0.000000  0.014394  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.013903        0.00000                         
TER    1786      ASP A 214                                                      
TER    3517      ASP B 214                                                      
MASTER      357    0    8   19   14    0    3    6 3954    2   88   36          
END                                                                             

Send your questions or comments to :
Mail to: Nicolas Lenfant, Thierry Hotelier, Yves Bourne, Pascale Marchot and Arnaud Chatonnet.
Please cite: Lenfant 2013 Nucleic.Acids.Res. or Marchot Chatonnet 2012 Prot.Pept Lett.
For technical information about these pages see:
ESTHER Home Page and ACEDB Home Page
AcePerl Lincoln Stein Home Page
webmaster

Acknowledgements and disclaimer