longtext: 8jh8-pdb

content
HEADER    HYDROLASE                               22-MAY-23   8JH8
TITLE     STRUCTURE-BASED CHARACTERIZATION AND IMPROVEMENT OF AN ENZYMATIC
TITLE    2 ACTIVITY OF ACREMONIUM ALCALOPHILUM FERULOYL ESTERASE
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: FERULOYL ESTERASE;
COMPND   3 CHAIN: A;
COMPND   4 EC: 3.1.1.73;
COMPND   5 ENGINEERED: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: SODIOMYCES ALCALOPHILUS;
SOURCE   3 ORGANISM_TAXID: 398408;
SOURCE   4 EXPRESSION_SYSTEM: KOMAGATAELLA PASTORIS;
SOURCE   5 EXPRESSION_SYSTEM_TAXID: 4922
KEYWDS    FERULOYL ESTERASE, HYDROLASE
EXPDTA    X-RAY DIFFRACTION
AUTHOR    A.PHIENLUPHON,K.KONDO,B.MIKAMI,T.NAGATA,M.KATAHIRA
REVDAT   1   17-APR-24 8JH8    0
JRNL        AUTH   A.PHIENLUPHON,K.KONDO,B.MIKAMI,K.S.K.TEO,K.SAITO,T.WATANABE,
JRNL        AUTH 2 T.NAGATA,M.KATAHIRA
JRNL        TITL   STRUCTURE-BASED CHARACTERIZATION AND IMPROVEMENT OF AN
JRNL        TITL 2 ENZYMATIC ACTIVITY OF ACREMONIUM ALCALOPHILUM FERULOYL
JRNL        TITL 3 ESTERASE
JRNL        REF    ACS SUSTAIN CHEM ENG          V.  12  3831 2024
JRNL        REFN                   ESSN 2168-0485
JRNL        DOI    10.1021/ACSSUSCHEMENG.3C08222
REMARK   2
REMARK   2 RESOLUTION.    1.55 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : PHENIX 1.20
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 : GEOSTD + MONOMER LIBRARY + CDL V1.2
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.55
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 37.78
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.350
REMARK   3   COMPLETENESS FOR RANGE        (%) : 96.2
REMARK   3   NUMBER OF REFLECTIONS             : 33128
REMARK   3
REMARK   3  FIT TO DATA USED IN REFINEMENT.
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.153
REMARK   3   R VALUE            (WORKING SET) : 0.149
REMARK   3   FREE R VALUE                     : 0.224
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000
REMARK   3   FREE R VALUE TEST SET COUNT      : 1657
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 37.7800 -  3.5400    1.00     2820   149  0.1232 0.1837
REMARK   3     2  3.5400 -  2.8100    0.99     2752   145  0.1400 0.2066
REMARK   3     3  2.8100 -  2.4600    1.00     2726   143  0.1562 0.2458
REMARK   3     4  2.4600 -  2.2300    1.00     2710   143  0.1532 0.2273
REMARK   3     5  2.2300 -  2.0700    1.00     2727   144  0.1639 0.2452
REMARK   3     6  2.0700 -  1.9500    1.00     2717   142  0.1616 0.2762
REMARK   3     7  1.9500 -  1.8500    1.00     2724   144  0.1677 0.2326
REMARK   3     8  1.8500 -  1.7700    1.00     2677   141  0.1740 0.2581
REMARK   3     9  1.7700 -  1.7000    1.00     2711   142  0.1890 0.2934
REMARK   3    10  1.7000 -  1.6400    0.98     2638   139  0.1880 0.2868
REMARK   3    11  1.6400 -  1.5900    0.86     2321   122  0.1986 0.2782
REMARK   3    12  1.5900 -  1.5500    0.72     1948   103  0.2234 0.2903
REMARK   3
REMARK   3  BULK SOLVENT MODELLING.
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL
REMARK   3   SOLVENT RADIUS     : 1.11
REMARK   3   SHRINKAGE RADIUS   : 0.90
REMARK   3   K_SOL              : NULL
REMARK   3   B_SOL              : NULL
REMARK   3
REMARK   3  ERROR ESTIMATES.
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.204
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 23.965
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : 21.64
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 31.14
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      :  0.005           1970
REMARK   3   ANGLE     :  0.734           2685
REMARK   3   CHIRALITY :  0.053            274
REMARK   3   PLANARITY :  0.006            367
REMARK   3   DIHEDRAL  : 13.980            717
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 8JH8 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 01-JUN-23.
REMARK 100 THE DEPOSITION ID IS D_1300037810.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 23-FEB-21
REMARK 200  TEMPERATURE           (KELVIN) : 100
REMARK 200  PH                             : 8.5
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : Y
REMARK 200  RADIATION SOURCE               : SPRING-8
REMARK 200  BEAMLINE                       : BL26B1
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0
REMARK 200  MONOCHROMATOR                  : NULL
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : PIXEL
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS EIGER X 4M
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS JAN10, 2022
REMARK 200  DATA SCALING SOFTWARE          : XDS JAN10, 2022
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 33128
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.550
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     (%) : 95.9
REMARK 200  DATA REDUNDANCY                : 5.230
REMARK 200  R MERGE                    (I) : 0.04700
REMARK 200  R SYM                      (I) : NULL
REMARK 200   FOR THE DATA SET  : 18.6100
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.55
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.64
REMARK 200  COMPLETENESS FOR SHELL     (%) : 95.9
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.46
REMARK 200  R MERGE FOR SHELL          (I) : 0.29300
REMARK 200  R SYM FOR SHELL            (I) : NULL
REMARK 200   FOR SHELL         : 2.840
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP 11.7.01
REMARK 200 STARTING MODEL: ALPHAFOLD
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 42.89
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.15
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M MGCL2, 0.1 M TRIS-HCL, 30% (W/V)
REMARK 280  PEG4,000, PH 8.5, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -X,Y,-Z
REMARK 290       3555   X+1/2,Y+1/2,Z
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        0.00000
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000
REMARK 290   SMTRY1   3  1.000000  0.000000  0.000000       49.75800
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       18.86900
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       49.75800
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       18.86900
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 APPLY THE FOLLOWING TO CHAINS: A, 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 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 MG    MG A 303  LIES ON A SPECIAL POSITION.
REMARK 375      HOH A 614  LIES ON A SPECIAL POSITION.
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    -5
REMARK 465     HIS A    -4
REMARK 465     HIS A    -3
REMARK 465     HIS A    -2
REMARK 465     HIS A    -1
REMARK 465     HIS A     0
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    SER A  51      -17.76     76.72
REMARK 500    SER A 119     -113.48     56.89
REMARK 500    ASN A 227       59.72    -93.26
REMARK 500
REMARK 500 REMARK: NULL
DBREF  8JH8 A   -5   242  PDB    8JH8     8JH8            -5    242
SEQRES   1 A  248  HIS HIS HIS HIS HIS HIS GLN ASN THR ALA GLY CYS GLY
SEQRES   2 A  248  GLN ASN PRO PRO SER SER GLY VAL LYS SER ILE ASN VAL
SEQRES   3 A  248  GLY GLY MET ASN ARG GLU TYR ILE LEU GLN LEU PRO ASN
SEQRES   4 A  248  ASN TYR ASP PRO ASN LYS GLY HIS MET LEU ILE PHE GLY
SEQRES   5 A  248  LEU HIS TRP LEU SER GLY SER MET HIS ASP VAL HIS PRO
SEQRES   6 A  248  ASN TYR TYR GLY LEU ARG GLN LEU ALA GLY ASN ASN ALA
SEQRES   7 A  248  ILE PHE ILE SER PRO ASN GLY ILE ASN ASN GLY TRP ALA
SEQRES   8 A  248  ASN ASP GLY GLY ARG ASP VAL ASN PHE ILE ASP ALA ILE
SEQRES   9 A  248  LEU GLN GLN VAL ARG SER GLN LEU CYS ILE ASN ASP SER
SEQRES  10 A  248  GLN ILE PHE ALA THR GLY PHE SER PHE GLY GLY GLY MET
SEQRES  11 A  248  SER TYR ALA LEU GLY CYS ALA ARG ALA ASN VAL PHE ARG
SEQRES  12 A  248  ALA ILE ALA PRO ILE ALA GLY ALA GLN ILE SER GLY CYS
SEQRES  13 A  248  SER GLY GLY THR SER PRO ILE ALA PHE LEU GLY ILE HIS
SEQRES  14 A  248  GLY THR ASN ASP ASP VAL LEU PRO ILE ALA MET GLY ARG
SEQRES  15 A  248  GLN VAL ARG ASP ARG PHE LEU GLN ASN ASN GLY CYS GLN
SEQRES  16 A  248  PRO LYS ASN ALA PRO GLU PRO GLY TRP GLY GLN GLY PRO
SEQRES  17 A  248  ILE LYS THR GLU TYR SER CYS GLN PRO ASN TYR PRO VAL
SEQRES  18 A  248  THR TRP ILE ALA PHE SER GLY GLY HIS ASP PRO ASN GLN
SEQRES  19 A  248  SER PHE VAL GLY ARG GLU ILE TRP ASP PHE PHE SER GLN
SEQRES  20 A  248  PHE
HET    NAG  B   1      14
HET    NAG  B   2      14
HET    PEG  A 301       7
HET     MG  A 302       1
HET     MG  A 303       1
HETNAM     NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE
HETNAM     PEG DI(HYDROXYETHYL)ETHER
HETNAM      MG MAGNESIUM ION
HETSYN     NAG N-ACETYL-BETA-D-GLUCOSAMINE; 2-ACETAMIDO-2-DEOXY-BETA-
HETSYN   2 NAG  D-GLUCOSE; 2-ACETAMIDO-2-DEOXY-D-GLUCOSE; 2-ACETAMIDO-
HETSYN   3 NAG  2-DEOXY-GLUCOSE; N-ACETYL-D-GLUCOSAMINE
FORMUL   2  NAG    2(C8 H15 N O6)
FORMUL   3  PEG    C4 H10 O3
FORMUL   4   MG    2(MG 2+)
FORMUL   6  HOH   *235(H2 O)
HELIX    1 AA1 SER A   53  HIS A   58  1                                   6
HELIX    2 AA2 ASN A   60  LEU A   64  5                                   5
HELIX    3 AA3 GLY A   79  GLY A   83  5                                   5
HELIX    4 AA4 ASN A   86  GLY A   88  5                                   3
HELIX    5 AA5 GLY A   89  LEU A  106  1                                  18
HELIX    6 AA6 SER A  119  ARG A  132  1                                  14
HELIX    7 AA7 PRO A  171  ASN A  186  1                                  16
HELIX    8 AA8 SER A  229  SER A  240  1                                  12
SHEET    1 AA1 9 GLY A  14  VAL A  20  0
SHEET    2 AA1 9 MET A  23  GLN A  30 -1  O  TYR A  27   N  LYS A  16
SHEET    3 AA1 9 ALA A  72  PRO A  77 -1  O  PHE A  74   N  GLN A  30
SHEET    4 AA1 9 HIS A  41  LEU A  47  1  N  MET A  42   O  ILE A  73
SHEET    5 AA1 9 ILE A 108  PHE A 118  1  O  PHE A 114   N  LEU A  43
SHEET    6 AA1 9 ALA A 138  ILE A 142  1  O  ILE A 142   N  GLY A 117
SHEET    7 AA1 9 ALA A 158  GLY A 164  1  O  LEU A 160   N  ILE A 139
SHEET    8 AA1 9 VAL A 215  PHE A 220  1  O  ILE A 218   N  GLY A 161
SHEET    9 AA1 9 ILE A 203  GLU A 206 -1  N  THR A 205   O  TRP A 217
SSBOND   1 CYS A    6    CYS A  107                          1555   1555  2.05
SSBOND   2 CYS A  130    CYS A  150                          1555   1555  2.05
SSBOND   3 CYS A  188    CYS A  209                          1555   1555  2.04
LINK         ND2 ASN A 109                 C1  NAG B   1     1555   1555  1.44
LINK         O4  NAG B   1                 C1  NAG B   2     1555   1555  1.45
LINK         OG  SER A 119                MG    MG A 302     1555   1555  2.91
CISPEP   1 HIS A   58    PRO A   59          0         0.28
CRYST1   99.516   37.738   77.709  90.00 125.93  90.00 C 1 2 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      0.010049  0.000000  0.007281        0.00000
SCALE2      0.000000  0.026498  0.000000        0.00000
SCALE3      0.000000  0.000000  0.015892        0.00000
TER    1877      PHE A 242
MASTER      240    0    5    8    9    0    0    6 2113    1   44   20
END