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PDBsum entry 1fgs

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Synthetase PDB id
1fgs
Jmol
Contents
Protein chain
393 a.a.
Ligands
POP
Metals
_MG
Waters ×169
HEADER    SYNTHETASE                              29-APR-98   1FGS
TITLE     FOLYLPOLYGLUTAMATE SYNTHETASE FROM LACTOBACILLUS CASEI
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: FOLYLPOLYGLUTAMATE SYNTHETASE;
COMPND   3 CHAIN: A;
COMPND   4 SYNONYM: FPGS;
COMPND   5 EC: 6.3.2.17;
COMPND   6 ENGINEERED: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: LACTOBACILLUS CASEI;
SOURCE   3 ORGANISM_TAXID: 1582;
SOURCE   4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE   5 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS    SYNTHETASE, LIGASE
EXPDTA    X-RAY DIFFRACTION
AUTHOR    X.SUN,A.BOGNAR,E.BAKER,C.SMITH
REVDAT   2   24-FEB-09 1FGS    1       VERSN
REVDAT   1   04-MAY-99 1FGS    0
JRNL        AUTH   X.SUN,A.L.BOGNAR,E.N.BAKER,C.A.SMITH
JRNL        TITL   STRUCTURAL HOMOLOGIES WITH ATP- AND FOLATE-BINDING
JRNL        TITL 2 ENZYMES IN THE CRYSTAL STRUCTURE OF
JRNL        TITL 3 FOLYLPOLYGLUTAMATE SYNTHETASE.
JRNL        REF    PROC.NATL.ACAD.SCI.USA        V.  95  6647 1998
JRNL        REFN                   ISSN 0027-8424
JRNL        PMID   9618466
JRNL        DOI    10.1073/PNAS.95.12.6647
REMARK   1
REMARK   2
REMARK   2 RESOLUTION.    2.40 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : TNT
REMARK   3   AUTHORS     : TRONRUD,TEN EYCK,MATTHEWS
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.40
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 15.00
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL
REMARK   3   COMPLETENESS FOR RANGE        (%) : NULL
REMARK   3   NUMBER OF REFLECTIONS             : 15311
REMARK   3
REMARK   3  USING DATA ABOVE SIGMA CUTOFF.
REMARK   3   CROSS-VALIDATION METHOD          : NULL
REMARK   3   FREE R VALUE TEST SET SELECTION  : NULL
REMARK   3   R VALUE     (WORKING + TEST SET) : NULL
REMARK   3   R VALUE            (WORKING SET) : NULL
REMARK   3   FREE R VALUE                     : NULL
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL
REMARK   3   FREE R VALUE TEST SET COUNT      : NULL
REMARK   3
REMARK   3  USING ALL DATA, NO SIGMA CUTOFF.
REMARK   3   R VALUE   (WORKING + TEST SET, NO CUTOFF) : NULL
REMARK   3   R VALUE          (WORKING SET, NO CUTOFF) : 0.1960
REMARK   3   FREE R VALUE                  (NO CUTOFF) : 0.265
REMARK   3   FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : 5.00
REMARK   3   FREE R VALUE TEST SET COUNT   (NO CUTOFF) : 809
REMARK   3   TOTAL NUMBER OF REFLECTIONS   (NO CUTOFF) : 16120
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 2988
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 10
REMARK   3   SOLVENT ATOMS            : 169
REMARK   3
REMARK   3  WILSON B VALUE (FROM FCALC, A**2) : NULL
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.    RMS    WEIGHT  COUNT
REMARK   3   BOND LENGTHS                 (A) : 0.008 ; NULL  ; NULL
REMARK   3   BOND ANGLES            (DEGREES) : 1.460 ; NULL  ; NULL
REMARK   3   TORSION ANGLES         (DEGREES) : NULL  ; NULL  ; NULL
REMARK   3   PSEUDOROTATION ANGLES  (DEGREES) : NULL  ; NULL  ; NULL
REMARK   3   TRIGONAL CARBON PLANES       (A) : NULL  ; NULL  ; NULL
REMARK   3   GENERAL PLANES               (A) : NULL  ; NULL  ; NULL
REMARK   3   ISOTROPIC THERMAL FACTORS (A**2) : NULL  ; NULL  ; NULL
REMARK   3   NON-BONDED CONTACTS          (A) : NULL  ; NULL  ; NULL
REMARK   3
REMARK   3  INCORRECT CHIRAL-CENTERS (COUNT) : NULL
REMARK   3
REMARK   3  BULK SOLVENT MODELING.
REMARK   3   METHOD USED : NULL
REMARK   3   KSOL        : NULL
REMARK   3   BSOL        : NULL
REMARK   3
REMARK   3  RESTRAINT LIBRARIES.
REMARK   3   STEREOCHEMISTRY : ENGH AND HUBER
REMARK   3   ISOTROPIC THERMAL FACTOR RESTRAINTS : NULL
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: NULL
REMARK   4
REMARK   4 1FGS COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 20-NOV-96
REMARK 200  TEMPERATURE           (KELVIN) : 285
REMARK 200  PH                             : 5.3
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : N
REMARK 200  RADIATION SOURCE               : ROTATING ANODE
REMARK 200  BEAMLINE                       : NULL
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU RUH2R
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418
REMARK 200  MONOCHROMATOR                  : NULL
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200  DATA SCALING SOFTWARE          : AGROVATA
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 15725
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.400
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     (%) : 100.0
REMARK 200  DATA REDUNDANCY                : 2.500
REMARK 200  R MERGE                    (I) : 0.07300
REMARK 200  R SYM                      (I) : NULL
REMARK 200   FOR THE DATA SET  : 9.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.40
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.50
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL
REMARK 200  R MERGE FOR SHELL          (I) : 0.27200
REMARK 200  R SYM FOR SHELL            (I) : NULL
REMARK 200   FOR SHELL         : 2.200
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: NULL
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MULTIPLE ISOMORPHOUS
REMARK 200  REPLACEMENT
REMARK 200 SOFTWARE USED: MLPHARE
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 53.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.62
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PH 5.3
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       23.05000
REMARK 290   SMTRY3   2  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 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     LYS A    18
REMARK 465     THR A    19
REMARK 465     ILE A   146
REMARK 465     GLY A   147
REMARK 465     GLY A   148
REMARK 465     ASP A   149
REMARK 465     THR A   150
REMARK 465     HIS A   170
REMARK 465     GLN A   171
REMARK 465     LYS A   172
REMARK 465     LEU A   173
REMARK 465     LEU A   174
REMARK 465     GLY A   175
REMARK 465     HIS A   176
REMARK 465     ILE A   342
REMARK 465     LEU A   343
REMARK 465     ALA A   344
REMARK 465     ASP A   345
REMARK 465     LYS A   346
REMARK 465     ASP A   347
REMARK 465     ALA A   373
REMARK 465     LEU A   374
REMARK 465     PRO A   375
REMARK 465     GLU A   376
REMARK 465     ALA A   377
REMARK 465     GLY A   378
REMARK 465     TYR A   379
REMARK 465     GLU A   380
REMARK 465     ALA A   381
REMARK 465     LEU A   382
REMARK 465     HIS A   383
REMARK 465     GLU A   384
REMARK 465     GLY A   426
REMARK 465     LYS A   427
REMARK 465     SER A   428
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     ARG A  15    CG   CD   NE   CZ   NH1  NH2
REMARK 470     ASP A  21    CG   OD1  OD2
REMARK 470     ASP A 169    CG   OD1  OD2
REMARK 470     ASN A 317    CG   OD1  ND2
REMARK 470     TYR A 348    CG   CD1  CD2  CE1  CE2  CZ   OH
REMARK 470     ASP A 353    CG   OD1  OD2
REMARK 470     ARG A 354    CG   CD   NE   CZ   NH1  NH2
REMARK 470     ARG A 372    CG   CD   NE   CZ   NH1  NH2
REMARK 470     TYR A 414    CG   CD1  CD2  CE1  CE2  CZ   OH
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    ASP A 244   CB  -  CG  -  OD1 ANGL. DEV. =   5.6 DEGREES
REMARK 500    PRO A 318   C   -  N   -  CD  ANGL. DEV. = -15.8 DEGREES
REMARK 500    PRO A 371   C   -  N   -  CD  ANGL. DEV. = -36.9 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    VAL A 155       14.61   -144.41
REMARK 500    ARG A 224      -62.64   -125.18
REMARK 500    TRP A 236       74.40   -105.17
REMARK 500    ASP A 244     -153.71   -142.94
REMARK 500    PRO A 255       51.44    -95.45
REMARK 500    SER A 360      -97.94    -67.15
REMARK 500    THR A 370     -168.94   -112.55
REMARK 500    PRO A 371     -103.52   -115.11
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 A 511        DISTANCE =  5.03 ANGSTROMS
REMARK 525    HOH A 561        DISTANCE =  5.43 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                              MG A 998  MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 POP A 999   O1
REMARK 620 2 SER A  73   O   159.5
REMARK 620 3 GLU A 143   OE1 130.3  68.7
REMARK 620 4 GLU A 143   OE2  93.0 100.9  42.6
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 MG A 998
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE POP A 999
DBREF  1FGS A    1   428  UNP    P15925   FOLC_LACCA       1    428
SEQADV 1FGS ALA A  128  UNP  P15925    GLY   128 CONFLICT
SEQRES   1 A  428  MET ASN TYR THR GLU THR VAL ALA TYR ILE HIS SER PHE
SEQRES   2 A  428  PRO ARG LEU ALA LYS THR GLY ASP HIS ARG ARG ILE LEU
SEQRES   3 A  428  THR LEU LEU HIS ALA LEU GLY ASN PRO GLN GLN GLN GLY
SEQRES   4 A  428  ARG TYR ILE HIS VAL THR GLY THR ASN GLY LYS GLY SER
SEQRES   5 A  428  ALA ALA ASN ALA ILE ALA HIS VAL LEU GLU ALA SER GLY
SEQRES   6 A  428  LEU THR VAL GLY LEU TYR THR SER PRO PHE ILE MET ARG
SEQRES   7 A  428  PHE ASN GLU ARG ILE MET ILE ASP HIS GLU PRO ILE PRO
SEQRES   8 A  428  ASP ALA ALA LEU VAL ASN ALA VAL ALA PHE VAL ARG ALA
SEQRES   9 A  428  ALA LEU GLU ARG LEU GLN GLN GLN GLN ALA ASP PHE ASN
SEQRES  10 A  428  VAL THR GLU PHE GLU PHE ILE THR ALA LEU ALA TYR TRP
SEQRES  11 A  428  TYR PHE ARG GLN ARG GLN VAL ASP VAL ALA VAL ILE GLU
SEQRES  12 A  428  VAL GLY ILE GLY GLY ASP THR ASP SER THR ASN VAL ILE
SEQRES  13 A  428  THR PRO VAL VAL SER VAL LEU THR GLU VAL ALA LEU ASP
SEQRES  14 A  428  HIS GLN LYS LEU LEU GLY HIS THR ILE THR ALA ILE ALA
SEQRES  15 A  428  LYS HIS LYS ALA GLY ILE ILE LYS ARG GLY ILE PRO VAL
SEQRES  16 A  428  VAL THR GLY ASN LEU VAL PRO ASP ALA ALA ALA VAL VAL
SEQRES  17 A  428  ALA ALA LYS VAL ALA THR THR GLY SER GLN TRP LEU ARG
SEQRES  18 A  428  PHE ASP ARG ASP PHE SER VAL PRO LYS ALA LYS LEU HIS
SEQRES  19 A  428  GLY TRP GLY GLN ARG PHE THR TYR GLU ASP GLN ASP GLY
SEQRES  20 A  428  ARG ILE SER ASP LEU GLU VAL PRO LEU VAL GLY ASP TYR
SEQRES  21 A  428  GLN GLN ARG ASN MET ALA ILE ALA ILE GLN THR ALA LYS
SEQRES  22 A  428  VAL TYR ALA LYS GLN THR GLU TRP PRO LEU THR PRO GLN
SEQRES  23 A  428  ASN ILE ARG GLN GLY LEU ALA ALA SER HIS TRP PRO ALA
SEQRES  24 A  428  ARG LEU GLU LYS ILE SER ASP THR PRO LEU ILE VAL ILE
SEQRES  25 A  428  ASP GLY ALA HIS ASN PRO ASP GLY ILE ASN GLY LEU ILE
SEQRES  26 A  428  THR ALA LEU LYS GLN LEU PHE SER GLN PRO ILE THR VAL
SEQRES  27 A  428  ILE ALA GLY ILE LEU ALA ASP LYS ASP TYR ALA ALA MET
SEQRES  28 A  428  ALA ASP ARG LEU THR ALA ALA PHE SER THR VAL TYR LEU
SEQRES  29 A  428  VAL PRO VAL PRO GLY THR PRO ARG ALA LEU PRO GLU ALA
SEQRES  30 A  428  GLY TYR GLU ALA LEU HIS GLU GLY ARG LEU LYS ASP SER
SEQRES  31 A  428  TRP GLN GLU ALA LEU ALA ALA SER LEU ASN ASP VAL PRO
SEQRES  32 A  428  ASP GLN PRO ILE VAL ILE THR GLY SER LEU TYR LEU ALA
SEQRES  33 A  428  SER ALA VAL ARG GLN THR LEU LEU GLY GLY LYS SER
HET     MG  A 998       1
HET    POP  A 999       9
HETNAM      MG MAGNESIUM ION
HETNAM     POP PYROPHOSPHATE 2-
FORMUL   2   MG    MG 2+
FORMUL   3  POP    H2 O7 P2 2-
FORMUL   4  HOH   *169(H2 O)
HELIX    1   1 TYR A    3  ILE A   10  1                                   8
HELIX    2   2 ARG A   23  ALA A   31  1                                   9
HELIX    3   3 PRO A   35  GLN A   37  5                                   3
HELIX    4   4 LYS A   50  ALA A   63  1                                  14
HELIX    5   5 PHE A   79  ARG A   82  5                                   4
HELIX    6   6 ASP A   92  GLN A  112  1                                  21
HELIX    7   7 GLU A  120  GLN A  134  1                                  15
HELIX    8   8 ILE A  178  ILE A  188  1                                  11
HELIX    9   9 PRO A  202  THR A  215  1                                  14
HELIX   10  10 ASP A  259  GLN A  278  5                                  20
HELIX   11  11 PRO A  285  ALA A  293  1                                   9
HELIX   12  12 PRO A  318  LEU A  331  1                                  14
HELIX   13  13 MET A  351  ALA A  358  1                                   8
HELIX   14  14 TRP A  391  ASP A  401  1                                  11
HELIX   15  15 LEU A  413  LEU A  423  1                                  11
SHEET    1   A 7 TRP A 219  ARG A 221  0
SHEET    2   A 7 PRO A 194  THR A 197  1  N  VAL A 195   O  LEU A 220
SHEET    3   A 7 VAL A 160  LEU A 163  1  N  SER A 161   O  PRO A 194
SHEET    4   A 7 TYR A  41  THR A  45  1  N  HIS A  43   O  VAL A 160
SHEET    5   A 7 VAL A 139  GLU A 143  1  N  ALA A 140   O  ILE A  42
SHEET    6   A 7 VAL A  68  TYR A  71  1  N  GLY A  69   O  VAL A 139
SHEET    7   A 7 ILE A  83  ILE A  85 -1  N  MET A  84   O  LEU A  70
SHEET    1   B 3 LYS A 230  LEU A 233  0
SHEET    2   B 3 GLN A 238  THR A 241 -1  N  THR A 241   O  LYS A 230
SHEET    3   B 3 LEU A 252  VAL A 254 -1  N  VAL A 254   O  GLN A 238
SHEET    1   C 5 THR A 361  LEU A 364  0
SHEET    2   C 5 ILE A 336  ALA A 340  1  N  VAL A 338   O  THR A 361
SHEET    3   C 5 PRO A 406  THR A 410  1  N  PRO A 406   O  THR A 337
SHEET    4   C 5 ILE A 310  ILE A 312  1  N  VAL A 311   O  ILE A 407
SHEET    5   C 5 GLU A 302  SER A 305 -1  N  SER A 305   O  ILE A 310
LINK        MG    MG A 998                 O1  POP A 999     1555   1555  3.04
LINK        MG    MG A 998                 O   SER A  73     1555   1555  2.48
LINK        MG    MG A 998                 OE1 GLU A 143     1555   1555  3.14
LINK        MG    MG A 998                 OE2 GLU A 143     1555   1555  2.63
CISPEP   1 SER A   73    PRO A   74          0         0.94
CISPEP   2 THR A  307    PRO A  308          0         3.20
SITE     1 AC1  3 SER A  73  GLU A 143  POP A 999
SITE     1 AC2  8 ASN A  48  GLY A  49  LYS A  50  GLY A  51
SITE     2 AC2  8 SER A  52  TRP A 297  ARG A 300   MG A 998
CRYST1   54.000   46.100   84.900  90.00 107.30  90.00 P 1 21 1      2
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      0.018519  0.000000  0.005768        0.00000
SCALE2      0.000000  0.021692  0.000000        0.00000
SCALE3      0.000000  0.000000  0.012337        0.00000
      
PROCHECK
Go to PROCHECK summary
 References