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Database: PDB
Entry: 5GL7
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Original site: 5GL7 
HEADER    LIGASE                                  08-JUL-16   5GL7              
TITLE     CRYSTAL STRUCTURE OF A TRUNCATED HUMAN CYTOSOLIC METHIONYL-TRNA       
TITLE    2 SYNTHETASE                                                           
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: METHIONINE--TRNA LIGASE, CYTOPLASMIC;                      
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: UNP RESIDUES 221-834;                                      
COMPND   5 SYNONYM: METHIONYL-TRNA SYNTHETASE,METRS;                            
COMPND   6 EC: 6.1.1.10;                                                        
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: MARS;                                                          
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID                               
KEYWDS    MSC, METRS, LIGASE                                                    
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    H.Y.CHO,H.J.LEE,B.S.KANG                                              
REVDAT   2   20-MAR-24 5GL7    1       REMARK                                   
REVDAT   1   12-JUL-17 5GL7    0                                                
JRNL        AUTH   H.Y.CHO,H.J.LEE,B.S.KANG                                     
JRNL        TITL   CRYSTAL STRUCTURE OF A TRUNCATED HUMAN CYTOSOLIC             
JRNL        TITL 2 METHIONYL-TRNA SYNTHETASE                                    
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.01 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX 1.9_1690                                      
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) : 2.01                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 37.28                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.340                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.2                           
REMARK   3   NUMBER OF REFLECTIONS             : 48889                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.196                           
REMARK   3   R VALUE            (WORKING SET) : 0.194                           
REMARK   3   FREE R VALUE                     : 0.226                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.090                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2000                            
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 37.2900 -  4.8492    0.98     3563   153  0.1597 0.1615        
REMARK   3     2  4.8492 -  3.8502    1.00     3460   147  0.1460 0.1891        
REMARK   3     3  3.8502 -  3.3639    1.00     3456   147  0.1744 0.2002        
REMARK   3     4  3.3639 -  3.0565    1.00     3403   145  0.1983 0.2343        
REMARK   3     5  3.0565 -  2.8375    0.99     3369   144  0.2140 0.2510        
REMARK   3     6  2.8375 -  2.6702    0.98     3349   142  0.2211 0.2798        
REMARK   3     7  2.6702 -  2.5365    0.98     3343   144  0.2298 0.2588        
REMARK   3     8  2.5365 -  2.4261    0.98     3303   140  0.2284 0.3090        
REMARK   3     9  2.4261 -  2.3327    0.98     3324   142  0.2364 0.2603        
REMARK   3    10  2.3327 -  2.2523    0.98     3291   140  0.2414 0.2619        
REMARK   3    11  2.2523 -  2.1818    0.98     3314   142  0.2414 0.2854        
REMARK   3    12  2.1818 -  2.1195    0.98     3296   141  0.2604 0.2925        
REMARK   3    13  2.1195 -  2.0637    0.98     3302   140  0.2698 0.3110        
REMARK   3    14  2.0637 -  2.0133    0.93     3116   133  0.2935 0.3135        
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)     : 0.240            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 23.810           
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      :  0.002           4910                                  
REMARK   3   ANGLE     :  0.698           6676                                  
REMARK   3   CHIRALITY :  0.028            732                                  
REMARK   3   PLANARITY :  0.003            865                                  
REMARK   3   DIHEDRAL  : 13.850           1806                                  
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 5GL7 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 20-JUL-16.                  
REMARK 100 THE DEPOSITION ID IS D_1300000956.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 20-MAR-16                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : PAL/PLS                            
REMARK 200  BEAMLINE                       : 5C (4A)                            
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9756                             
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 : NULL                               
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 48954                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.013                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.2                               
REMARK 200  DATA REDUNDANCY                : 6.700                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 26.1000                            
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: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHENIX 1.9_1690                                       
REMARK 200 STARTING MODEL: ZINC PHAZING MODEL                                   
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 52.70                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.60                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 100MM TRIS PH 7.5, 200MM MAGNESIUM       
REMARK 280  CHLORIDE, 5MM DTT, 21% PEG 8000, VAPOR DIFFUSION, SITTING DROP,     
REMARK 280  TEMPERATURE 294K                                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-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       32.51750            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       61.04200            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       46.51500            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       61.04200            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       32.51750            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       46.51500            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 10 ANGSTROM**2                            
REMARK 350 SURFACE AREA OF THE COMPLEX: 25990 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -3.0 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 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     MET A   219                                                      
REMARK 465     SER A   220                                                      
REMARK 465     GLU A   221                                                      
REMARK 465     GLU A   222                                                      
REMARK 465     GLU A   223                                                      
REMARK 465     GLU A   224                                                      
REMARK 465     LEU A   225                                                      
REMARK 465     LYS A   823                                                      
REMARK 465     THR A   824                                                      
REMARK 465     SER A   825                                                      
REMARK 465     PRO A   826                                                      
REMARK 465     LYS A   827                                                      
REMARK 465     PRO A   828                                                      
REMARK 465     ALA A   829                                                      
REMARK 465     VAL A   830                                                      
REMARK 465     VAL A   831                                                      
REMARK 465     GLU A   832                                                      
REMARK 465     THR A   833                                                      
REMARK 465     VAL A   834                                                      
REMARK 465     LEU A   835                                                      
REMARK 465     GLU A   836                                                      
REMARK 465     HIS A   837                                                      
REMARK 465     HIS A   838                                                      
REMARK 465     HIS A   839                                                      
REMARK 465     HIS A   840                                                      
REMARK 465     HIS A   841                                                      
REMARK 465     HIS A   842                                                      
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     LEU A 250    CG   CD1  CD2                                       
REMARK 470     GLN A 253    CG   CD   OE1  NE2                                  
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   OD1  ASP A   555     OH   TYR A   586              2.12            
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  1087     O    HOH A  1149     1545     2.19            
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    PRO A 249       98.63    -59.06                                   
REMARK 500    CYS A 287      -83.41   -127.78                                   
REMARK 500    ASN A 542       63.05   -153.78                                   
REMARK 500    LEU A 562      -61.80   -120.48                                   
REMARK 500    GLU A 585     -166.34    -78.64                                   
REMARK 500    GLU A 590     -116.72     52.31                                   
REMARK 500    ASN A 649      -80.65   -125.05                                   
REMARK 500    LEU A 789       79.82   -116.81                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
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                              ZN A 901  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A 389   SG                                                     
REMARK 620 2 CYS A 392   SG  104.2                                              
REMARK 620 3 CYS A 435   SG  120.6 119.8                                        
REMARK 620 4 CYS A 438   SG   90.6 105.0 112.0                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A 902  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A 405   SG                                                     
REMARK 620 2 CYS A 408   SG  111.2                                              
REMARK 620 3 CYS A 418   SG  104.1 107.6                                        
REMARK 620 4 CYS A 421   SG  109.9 115.1 108.2                                  
REMARK 620 N                    1     2     3                                   
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 901                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 902                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 903                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 904                 
DBREF  5GL7 A  221   834  UNP    P56192   SYMC_HUMAN     221    834             
SEQADV 5GL7 MET A  219  UNP  P56192              EXPRESSION TAG                 
SEQADV 5GL7 SER A  220  UNP  P56192              EXPRESSION TAG                 
SEQADV 5GL7 LEU A  835  UNP  P56192              EXPRESSION TAG                 
SEQADV 5GL7 GLU A  836  UNP  P56192              EXPRESSION TAG                 
SEQADV 5GL7 HIS A  837  UNP  P56192              EXPRESSION TAG                 
SEQADV 5GL7 HIS A  838  UNP  P56192              EXPRESSION TAG                 
SEQADV 5GL7 HIS A  839  UNP  P56192              EXPRESSION TAG                 
SEQADV 5GL7 HIS A  840  UNP  P56192              EXPRESSION TAG                 
SEQADV 5GL7 HIS A  841  UNP  P56192              EXPRESSION TAG                 
SEQADV 5GL7 HIS A  842  UNP  P56192              EXPRESSION TAG                 
SEQRES   1 A  624  MET SER GLU GLU GLU GLU LEU ALA THR LEU SER GLU GLU          
SEQRES   2 A  624  GLU ILE ALA MET ALA VAL THR ALA TRP GLU LYS GLY LEU          
SEQRES   3 A  624  GLU SER LEU PRO PRO LEU ARG PRO GLN GLN ASN PRO VAL          
SEQRES   4 A  624  LEU PRO VAL ALA GLY GLU ARG ASN VAL LEU ILE THR SER          
SEQRES   5 A  624  ALA LEU PRO TYR VAL ASN ASN VAL PRO HIS LEU GLY ASN          
SEQRES   6 A  624  ILE ILE GLY CYS VAL LEU SER ALA ASP VAL PHE ALA ARG          
SEQRES   7 A  624  TYR SER ARG LEU ARG GLN TRP ASN THR LEU TYR LEU CYS          
SEQRES   8 A  624  GLY THR ASP GLU TYR GLY THR ALA THR GLU THR LYS ALA          
SEQRES   9 A  624  LEU GLU GLU GLY LEU THR PRO GLN GLU ILE CYS ASP LYS          
SEQRES  10 A  624  TYR HIS ILE ILE HIS ALA ASP ILE TYR ARG TRP PHE ASN          
SEQRES  11 A  624  ILE SER PHE ASP ILE PHE GLY ARG THR THR THR PRO GLN          
SEQRES  12 A  624  GLN THR LYS ILE THR GLN ASP ILE PHE GLN GLN LEU LEU          
SEQRES  13 A  624  LYS ARG GLY PHE VAL LEU GLN ASP THR VAL GLU GLN LEU          
SEQRES  14 A  624  ARG CYS GLU HIS CYS ALA ARG PHE LEU ALA ASP ARG PHE          
SEQRES  15 A  624  VAL GLU GLY VAL CYS PRO PHE CYS GLY TYR GLU GLU ALA          
SEQRES  16 A  624  ARG GLY ASP GLN CYS ASP LYS CYS GLY LYS LEU ILE ASN          
SEQRES  17 A  624  ALA VAL GLU LEU LYS LYS PRO GLN CYS LYS VAL CYS ARG          
SEQRES  18 A  624  SER CYS PRO VAL VAL GLN SER SER GLN HIS LEU PHE LEU          
SEQRES  19 A  624  ASP LEU PRO LYS LEU GLU LYS ARG LEU GLU GLU TRP LEU          
SEQRES  20 A  624  GLY ARG THR LEU PRO GLY SER ASP TRP THR PRO ASN ALA          
SEQRES  21 A  624  GLN PHE ILE THR ARG SER TRP LEU ARG ASP GLY LEU LYS          
SEQRES  22 A  624  PRO ARG CYS ILE THR ARG ASP LEU LYS TRP GLY THR PRO          
SEQRES  23 A  624  VAL PRO LEU GLU GLY PHE GLU ASP LYS VAL PHE TYR VAL          
SEQRES  24 A  624  TRP PHE ASP ALA THR ILE GLY TYR LEU SER ILE THR ALA          
SEQRES  25 A  624  ASN TYR THR ASP GLN TRP GLU ARG TRP TRP LYS ASN PRO          
SEQRES  26 A  624  GLU GLN VAL ASP LEU TYR GLN PHE MET ALA LYS ASP ASN          
SEQRES  27 A  624  VAL PRO PHE HIS SER LEU VAL PHE PRO CYS SER ALA LEU          
SEQRES  28 A  624  GLY ALA GLU ASP ASN TYR THR LEU VAL SER HIS LEU ILE          
SEQRES  29 A  624  ALA THR GLU TYR LEU ASN TYR GLU ASP GLY LYS PHE SER          
SEQRES  30 A  624  LYS SER ARG GLY VAL GLY VAL PHE GLY ASP MET ALA GLN          
SEQRES  31 A  624  ASP THR GLY ILE PRO ALA ASP ILE TRP ARG PHE TYR LEU          
SEQRES  32 A  624  LEU TYR ILE ARG PRO GLU GLY GLN ASP SER ALA PHE SER          
SEQRES  33 A  624  TRP THR ASP LEU LEU LEU LYS ASN ASN SER GLU LEU LEU          
SEQRES  34 A  624  ASN ASN LEU GLY ASN PHE ILE ASN ARG ALA GLY MET PHE          
SEQRES  35 A  624  VAL SER LYS PHE PHE GLY GLY TYR VAL PRO GLU MET VAL          
SEQRES  36 A  624  LEU THR PRO ASP ASP GLN ARG LEU LEU ALA HIS VAL THR          
SEQRES  37 A  624  LEU GLU LEU GLN HIS TYR HIS GLN LEU LEU GLU LYS VAL          
SEQRES  38 A  624  ARG ILE ARG ASP ALA LEU ARG SER ILE LEU THR ILE SER          
SEQRES  39 A  624  ARG HIS GLY ASN GLN TYR ILE GLN VAL ASN GLU PRO TRP          
SEQRES  40 A  624  LYS ARG ILE LYS GLY SER GLU ALA ASP ARG GLN ARG ALA          
SEQRES  41 A  624  GLY THR VAL THR GLY LEU ALA VAL ASN ILE ALA ALA LEU          
SEQRES  42 A  624  LEU SER VAL MET LEU GLN PRO TYR MET PRO THR VAL SER          
SEQRES  43 A  624  ALA THR ILE GLN ALA GLN LEU GLN LEU PRO PRO PRO ALA          
SEQRES  44 A  624  CYS SER ILE LEU LEU THR ASN PHE LEU CYS THR LEU PRO          
SEQRES  45 A  624  ALA GLY HIS GLN ILE GLY THR VAL SER PRO LEU PHE GLN          
SEQRES  46 A  624  LYS LEU GLU ASN ASP GLN ILE GLU SER LEU ARG GLN ARG          
SEQRES  47 A  624  PHE GLY GLY GLY GLN ALA LYS THR SER PRO LYS PRO ALA          
SEQRES  48 A  624  VAL VAL GLU THR VAL LEU GLU HIS HIS HIS HIS HIS HIS          
HET     ZN  A 901       1                                                       
HET     ZN  A 902       1                                                       
HET    GOL  A 903       6                                                       
HET    GOL  A 904       6                                                       
HETNAM      ZN ZINC ION                                                         
HETNAM     GOL GLYCEROL                                                         
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   2   ZN    2(ZN 2+)                                                     
FORMUL   4  GOL    2(C3 H8 O3)                                                  
FORMUL   6  HOH   *345(H2 O)                                                    
HELIX    1 AA1 SER A  229  LYS A  242  1                                  14    
HELIX    2 AA2 GLY A  243  LEU A  247  5                                   5    
HELIX    3 AA3 HIS A  280  CYS A  287  1                                   8    
HELIX    4 AA4 CYS A  287  ARG A  301  1                                  15    
HELIX    5 AA5 GLY A  315  GLU A  325  1                                  11    
HELIX    6 AA6 THR A  328  PHE A  347  1                                  20    
HELIX    7 AA7 THR A  359  LYS A  375  1                                  17    
HELIX    8 AA8 ALA A  397  ARG A  399  5                                   3    
HELIX    9 AA9 ASN A  426  LEU A  430  5                                   5    
HELIX   10 AB1 ASP A  453  LEU A  469  1                                  17    
HELIX   11 AB2 THR A  475  GLY A  489  1                                  15    
HELIX   12 AB3 TYR A  516  ALA A  521  1                                   6    
HELIX   13 AB4 ILE A  523  THR A  533  1                                  11    
HELIX   14 AB5 TRP A  536  LYS A  541  1                                   6    
HELIX   15 AB6 ASN A  556  LEU A  562  1                                   7    
HELIX   16 AB7 LEU A  562  GLU A  572  1                                  11    
HELIX   17 AB8 MET A  606  GLY A  611  5                                   6    
HELIX   18 AB9 PRO A  613  ILE A  624  1                                  12    
HELIX   19 AC1 SER A  634  LEU A  646  1                                  13    
HELIX   20 AC2 ASN A  649  PHE A  665  1                                  17    
HELIX   21 AC3 THR A  675  GLU A  697  1                                  23    
HELIX   22 AC4 ARG A  700  GLU A  723  1                                  24    
HELIX   23 AC5 GLU A  723  ILE A  728  1                                   6    
HELIX   24 AC6 SER A  731  LEU A  756  1                                  26    
HELIX   25 AC7 MET A  760  GLN A  772  1                                  13    
HELIX   26 AC8 PRO A  774  SER A  779  1                                   6    
HELIX   27 AC9 GLU A  806  PHE A  817  1                                  12    
SHEET    1 AA1 5 ILE A 353  ARG A 356  0                                        
SHEET    2 AA1 5 ASN A 304  THR A 311  1  N  CYS A 309   O  GLY A 355           
SHEET    3 AA1 5 ASN A 265  SER A 270  1  N  ILE A 268   O  LEU A 306           
SHEET    4 AA1 5 VAL A 546  ALA A 553  1  O  TYR A 549   N  LEU A 267           
SHEET    5 AA1 5 VAL A 578  THR A 584  1  O  ILE A 582   N  GLN A 550           
SHEET    1 AA2 4 ARG A 394  PHE A 395  0                                        
SHEET    2 AA2 4 VAL A 379  CYS A 389 -1  N  CYS A 389   O  ARG A 394           
SHEET    3 AA2 4 VAL A 443  LEU A 452 -1  O  PHE A 451   N  LEU A 380           
SHEET    4 AA2 4 ARG A 493  CYS A 494 -1  O  ARG A 493   N  LEU A 452           
SHEET    1 AA3 3 ALA A 413  ARG A 414  0                                        
SHEET    2 AA3 3 VAL A 401  VAL A 404 -1  N  GLY A 403   O  ALA A 413           
SHEET    3 AA3 3 LYS A 431  CYS A 435 -1  O  LYS A 431   N  VAL A 404           
SHEET    1 AA4 2 THR A 496  ARG A 497  0                                        
SHEET    2 AA4 2 VAL A 514  PHE A 515 -1  O  VAL A 514   N  ARG A 497           
SHEET    1 AA5 2 LEU A 587  TYR A 589  0                                        
SHEET    2 AA5 2 SER A 631  PHE A 633  1  O  PHE A 633   N  ASN A 588           
LINK         SG  CYS A 389                ZN    ZN A 901     1555   1555  2.19  
LINK         SG  CYS A 392                ZN    ZN A 901     1555   1555  2.45  
LINK         SG  CYS A 405                ZN    ZN A 902     1555   1555  2.33  
LINK         SG  CYS A 408                ZN    ZN A 902     1555   1555  2.33  
LINK         SG  CYS A 418                ZN    ZN A 902     1555   1555  2.40  
LINK         SG  CYS A 421                ZN    ZN A 902     1555   1555  2.36  
LINK         SG  CYS A 435                ZN    ZN A 901     1555   1555  2.38  
LINK         SG  CYS A 438                ZN    ZN A 901     1555   1555  2.51  
CISPEP   1 ASN A  255    PRO A  256          0         3.43                     
SITE     1 AC1  4 CYS A 389  CYS A 392  CYS A 435  CYS A 438                    
SITE     1 AC2  4 CYS A 405  CYS A 408  CYS A 418  CYS A 421                    
SITE     1 AC3  3 ARG A 299  GLN A 302  SER A 779                               
SITE     1 AC4  6 GLU A 263  GLN A 381  ASP A 382  THR A 383                    
SITE     2 AC4  6 HOH A1122  HOH A1176                                          
CRYST1   65.035   93.030  122.084  90.00  90.00  90.00 P 21 21 21    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      0.015376  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.010749  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.008191        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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