longtext: 8ytw-pdb

content
HEADER    HYDROLASE                               26-MAR-24   8YTW
TITLE     KUBU-PETASE FROM KUTZNERIA BURIRAMENSIS
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: DIENELACTONE HYDROLASE;
COMPND   3 CHAIN: A;
COMPND   4 ENGINEERED: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: KUTZNERIA BURIRAMENSIS;
SOURCE   3 ORGANISM_TAXID: 1045776;
SOURCE   4 GENE: BCF44_11928;
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE   7 EXPRESSION_SYSTEM_VARIANT: -T1R
KEYWDS    PET HYDROLASE, HYDROLASE
EXPDTA    X-RAY DIFFRACTION
AUTHOR    J.PARK,H.SEO,H.HONG,K.-J.KIM
REVDAT   1   15-JAN-25 8YTW    0
JRNL        AUTH   H.SEO,H.HONG,J.PARK,S.H.LEE,D.KI,A.RYU,H.Y.SAGONG,K.J.KIM
JRNL        TITL   LANDSCAPE PROFILING OF PET DEPOLYMERASES USING A NATURAL
JRNL        TITL 2 SEQUENCE CLUSTER FRAMEWORK.
JRNL        REF    SCIENCE                       V. 387 P5637 2025
JRNL        REFN                   ESSN 1095-9203
JRNL        PMID   39745946
JRNL        DOI    10.1126/SCIENCE.ADP5637
REMARK   2
REMARK   2 RESOLUTION.    2.65 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : REFMAC 5.8.0411
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK   3               : NICHOLLS,WINN,LONG,VAGIN
REMARK   3
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.65
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 45.88
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.9
REMARK   3   NUMBER OF REFLECTIONS             : 9707
REMARK   3
REMARK   3  FIT TO DATA USED IN REFINEMENT.
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.220
REMARK   3   R VALUE            (WORKING SET) : 0.217
REMARK   3   FREE R VALUE                     : 0.283
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000
REMARK   3   FREE R VALUE TEST SET COUNT      : 515
REMARK   3
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.
REMARK   3   TOTAL NUMBER OF BINS USED           : 20
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.65
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.72
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 685
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 100.0
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2350
REMARK   3   BIN FREE R VALUE SET COUNT          : 35
REMARK   3   BIN FREE R VALUE                    : 0.2880
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 1793
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 0
REMARK   3   SOLVENT ATOMS            : 0
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : NULL
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 59.45
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : 0.00000
REMARK   3    B22 (A**2) : 0.00000
REMARK   3    B33 (A**2) : 0.00000
REMARK   3    B12 (A**2) : 0.00000
REMARK   3    B13 (A**2) : 0.00000
REMARK   3    B23 (A**2) : 0.00000
REMARK   3
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.
REMARK   3   ESU BASED ON R VALUE                            (A): 0.492
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.328
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.213
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 9.993
REMARK   3
REMARK   3 CORRELATION COEFFICIENTS.
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.919
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.878
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  1845 ; 0.008 ; 0.011
REMARK   3   BOND LENGTHS OTHERS               (A):  1692 ; 0.001 ; 0.016
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  2530 ; 1.456 ; 1.637
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  3883 ; 0.492 ; 1.557
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   245 ; 7.213 ; 5.000
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):     9 ;11.118 ; 5.000
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   232 ;15.425 ;10.000
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):  NULL ;  NULL ;  NULL
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   285 ; 0.060 ; 0.200
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  2199 ; 0.007 ; 0.020
REMARK   3   GENERAL PLANES OTHERS             (A):   441 ; 0.001 ; 0.020
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL
REMARK   3
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):   986 ; 4.536 ; 5.851
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):   986 ; 4.532 ; 5.853
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  1229 ; 6.410 ;10.524
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  1230 ; 6.427 ;10.527
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):   859 ; 5.170 ; 6.160
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):   860 ; 5.167 ; 6.166
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  1302 ; 7.259 ;11.186
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  2026 ; 8.137 ;55.000
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  2027 ; 8.142 ;55.010
REMARK   3
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL
REMARK   3
REMARK   3  NCS RESTRAINTS STATISTICS
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK   3
REMARK   3  TLS DETAILS
REMARK   3   NUMBER OF TLS GROUPS  : NULL
REMARK   3
REMARK   3  BULK SOLVENT MODELLING.
REMARK   3   METHOD USED : MASK
REMARK   3   PARAMETERS FOR MASK CALCULATION
REMARK   3   VDW PROBE RADIUS   : 1.20
REMARK   3   ION PROBE RADIUS   : 0.80
REMARK   3   SHRINKAGE RADIUS   : 0.80
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK   3  POSITIONS
REMARK   4
REMARK   4 8YTW COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 27-MAR-24.
REMARK 100 THE DEPOSITION ID IS D_1300046370.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 24-JUN-23
REMARK 200  TEMPERATURE           (KELVIN) : 100
REMARK 200  PH                             : 6.4
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : Y
REMARK 200  RADIATION SOURCE               : PAL/PLS
REMARK 200  BEAMLINE                       : 7A (6B, 6C1)
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97934
REMARK 200  MONOCHROMATOR                  : DCM SI (111) CRYSTAL
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : CCD
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 270
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200  DATA SCALING SOFTWARE          : AIMLESS
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 9707
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.650
REMARK 200  RESOLUTION RANGE LOW       (A) : 45.880
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.9
REMARK 200  DATA REDUNDANCY                : 14.90
REMARK 200  R MERGE                    (I) : NULL
REMARK 200  R SYM                      (I) : NULL
REMARK 200   FOR THE DATA SET  : 26.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.65
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.72
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   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: MOLREP
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 60.28
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.10
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 300, IMIDAZOLE, ZINC ACETATE, PH
REMARK 280  6.4, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 41 3 2
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       5555   Z,X,Y
REMARK 290       6555   Z+1/2,-X+1/2,-Y
REMARK 290       7555   -Z+1/2,-X,Y+1/2
REMARK 290       8555   -Z,X+1/2,-Y+1/2
REMARK 290       9555   Y,Z,X
REMARK 290      10555   -Y,Z+1/2,-X+1/2
REMARK 290      11555   Y+1/2,-Z+1/2,-X
REMARK 290      12555   -Y+1/2,-Z,X+1/2
REMARK 290      13555   Y+3/4,X+1/4,-Z+1/4
REMARK 290      14555   -Y+3/4,-X+3/4,-Z+3/4
REMARK 290      15555   Y+1/4,-X+1/4,Z+3/4
REMARK 290      16555   -Y+1/4,X+3/4,Z+1/4
REMARK 290      17555   X+3/4,Z+1/4,-Y+1/4
REMARK 290      18555   -X+1/4,Z+3/4,Y+1/4
REMARK 290      19555   -X+3/4,-Z+3/4,-Y+3/4
REMARK 290      20555   X+1/4,-Z+1/4,Y+3/4
REMARK 290      21555   Z+3/4,Y+1/4,-X+1/4
REMARK 290      22555   Z+1/4,-Y+1/4,X+3/4
REMARK 290      23555   -Z+1/4,Y+3/4,X+1/4
REMARK 290      24555   -Z+3/4,-Y+3/4,-X+3/4
REMARK 290      25555   X+1/2,Y+1/2,Z+1/2
REMARK 290      26555   -X,-Y+1/2,Z
REMARK 290      27555   -X+1/2,Y,-Z
REMARK 290      28555   X,-Y,-Z+1/2
REMARK 290      29555   Z+1/2,X+1/2,Y+1/2
REMARK 290      30555   Z,-X,-Y+1/2
REMARK 290      31555   -Z,-X+1/2,Y
REMARK 290      32555   -Z+1/2,X,-Y
REMARK 290      33555   Y+1/2,Z+1/2,X+1/2
REMARK 290      34555   -Y+1/2,Z,-X
REMARK 290      35555   Y,-Z,-X+1/2
REMARK 290      36555   -Y,-Z+1/2,X
REMARK 290      37555   Y+1/4,X+3/4,-Z+3/4
REMARK 290      38555   -Y+1/4,-X+1/4,-Z+1/4
REMARK 290      39555   Y+3/4,-X+3/4,Z+1/4
REMARK 290      40555   -Y+3/4,X+1/4,Z+3/4
REMARK 290      41555   X+1/4,Z+3/4,-Y+3/4
REMARK 290      42555   -X+3/4,Z+1/4,Y+3/4
REMARK 290      43555   -X+1/4,-Z+1/4,-Y+1/4
REMARK 290      44555   X+3/4,-Z+3/4,Y+1/4
REMARK 290      45555   Z+1/4,Y+3/4,-X+3/4
REMARK 290      46555   Z+3/4,-Y+3/4,X+1/4
REMARK 290      47555   -Z+3/4,Y+1/4,X+3/4
REMARK 290      48555   -Z+1/4,-Y+1/4,-X+1/4
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       79.39500
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       79.39500
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       79.39500
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       79.39500
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       79.39500
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       79.39500
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000
REMARK 290   SMTRY1   5  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY2   5  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY3   5  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY1   6  0.000000  0.000000  1.000000       79.39500
REMARK 290   SMTRY2   6 -1.000000  0.000000  0.000000       79.39500
REMARK 290   SMTRY3   6  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY1   7  0.000000  0.000000 -1.000000       79.39500
REMARK 290   SMTRY2   7 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY3   7  0.000000  1.000000  0.000000       79.39500
REMARK 290   SMTRY1   8  0.000000  0.000000 -1.000000        0.00000
REMARK 290   SMTRY2   8  1.000000  0.000000  0.000000       79.39500
REMARK 290   SMTRY3   8  0.000000 -1.000000  0.000000       79.39500
REMARK 290   SMTRY1   9  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY2   9  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY3   9  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY1  10  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY2  10  0.000000  0.000000  1.000000       79.39500
REMARK 290   SMTRY3  10 -1.000000  0.000000  0.000000       79.39500
REMARK 290   SMTRY1  11  0.000000  1.000000  0.000000       79.39500
REMARK 290   SMTRY2  11  0.000000  0.000000 -1.000000       79.39500
REMARK 290   SMTRY3  11 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY1  12  0.000000 -1.000000  0.000000       79.39500
REMARK 290   SMTRY2  12  0.000000  0.000000 -1.000000        0.00000
REMARK 290   SMTRY3  12  1.000000  0.000000  0.000000       79.39500
REMARK 290   SMTRY1  13  0.000000  1.000000  0.000000      119.09250
REMARK 290   SMTRY2  13  1.000000  0.000000  0.000000       39.69750
REMARK 290   SMTRY3  13  0.000000  0.000000 -1.000000       39.69750
REMARK 290   SMTRY1  14  0.000000 -1.000000  0.000000      119.09250
REMARK 290   SMTRY2  14 -1.000000  0.000000  0.000000      119.09250
REMARK 290   SMTRY3  14  0.000000  0.000000 -1.000000      119.09250
REMARK 290   SMTRY1  15  0.000000  1.000000  0.000000       39.69750
REMARK 290   SMTRY2  15 -1.000000  0.000000  0.000000       39.69750
REMARK 290   SMTRY3  15  0.000000  0.000000  1.000000      119.09250
REMARK 290   SMTRY1  16  0.000000 -1.000000  0.000000       39.69750
REMARK 290   SMTRY2  16  1.000000  0.000000  0.000000      119.09250
REMARK 290   SMTRY3  16  0.000000  0.000000  1.000000       39.69750
REMARK 290   SMTRY1  17  1.000000  0.000000  0.000000      119.09250
REMARK 290   SMTRY2  17  0.000000  0.000000  1.000000       39.69750
REMARK 290   SMTRY3  17  0.000000 -1.000000  0.000000       39.69750
REMARK 290   SMTRY1  18 -1.000000  0.000000  0.000000       39.69750
REMARK 290   SMTRY2  18  0.000000  0.000000  1.000000      119.09250
REMARK 290   SMTRY3  18  0.000000  1.000000  0.000000       39.69750
REMARK 290   SMTRY1  19 -1.000000  0.000000  0.000000      119.09250
REMARK 290   SMTRY2  19  0.000000  0.000000 -1.000000      119.09250
REMARK 290   SMTRY3  19  0.000000 -1.000000  0.000000      119.09250
REMARK 290   SMTRY1  20  1.000000  0.000000  0.000000       39.69750
REMARK 290   SMTRY2  20  0.000000  0.000000 -1.000000       39.69750
REMARK 290   SMTRY3  20  0.000000  1.000000  0.000000      119.09250
REMARK 290   SMTRY1  21  0.000000  0.000000  1.000000      119.09250
REMARK 290   SMTRY2  21  0.000000  1.000000  0.000000       39.69750
REMARK 290   SMTRY3  21 -1.000000  0.000000  0.000000       39.69750
REMARK 290   SMTRY1  22  0.000000  0.000000  1.000000       39.69750
REMARK 290   SMTRY2  22  0.000000 -1.000000  0.000000       39.69750
REMARK 290   SMTRY3  22  1.000000  0.000000  0.000000      119.09250
REMARK 290   SMTRY1  23  0.000000  0.000000 -1.000000       39.69750
REMARK 290   SMTRY2  23  0.000000  1.000000  0.000000      119.09250
REMARK 290   SMTRY3  23  1.000000  0.000000  0.000000       39.69750
REMARK 290   SMTRY1  24  0.000000  0.000000 -1.000000      119.09250
REMARK 290   SMTRY2  24  0.000000 -1.000000  0.000000      119.09250
REMARK 290   SMTRY3  24 -1.000000  0.000000  0.000000      119.09250
REMARK 290   SMTRY1  25  1.000000  0.000000  0.000000       79.39500
REMARK 290   SMTRY2  25  0.000000  1.000000  0.000000       79.39500
REMARK 290   SMTRY3  25  0.000000  0.000000  1.000000       79.39500
REMARK 290   SMTRY1  26 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2  26  0.000000 -1.000000  0.000000       79.39500
REMARK 290   SMTRY3  26  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1  27 -1.000000  0.000000  0.000000       79.39500
REMARK 290   SMTRY2  27  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY3  27  0.000000  0.000000 -1.000000        0.00000
REMARK 290   SMTRY1  28  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2  28  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3  28  0.000000  0.000000 -1.000000       79.39500
REMARK 290   SMTRY1  29  0.000000  0.000000  1.000000       79.39500
REMARK 290   SMTRY2  29  1.000000  0.000000  0.000000       79.39500
REMARK 290   SMTRY3  29  0.000000  1.000000  0.000000       79.39500
REMARK 290   SMTRY1  30  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY2  30 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY3  30  0.000000 -1.000000  0.000000       79.39500
REMARK 290   SMTRY1  31  0.000000  0.000000 -1.000000        0.00000
REMARK 290   SMTRY2  31 -1.000000  0.000000  0.000000       79.39500
REMARK 290   SMTRY3  31  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY1  32  0.000000  0.000000 -1.000000       79.39500
REMARK 290   SMTRY2  32  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY3  32  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY1  33  0.000000  1.000000  0.000000       79.39500
REMARK 290   SMTRY2  33  0.000000  0.000000  1.000000       79.39500
REMARK 290   SMTRY3  33  1.000000  0.000000  0.000000       79.39500
REMARK 290   SMTRY1  34  0.000000 -1.000000  0.000000       79.39500
REMARK 290   SMTRY2  34  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY3  34 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY1  35  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY2  35  0.000000  0.000000 -1.000000        0.00000
REMARK 290   SMTRY3  35 -1.000000  0.000000  0.000000       79.39500
REMARK 290   SMTRY1  36  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY2  36  0.000000  0.000000 -1.000000       79.39500
REMARK 290   SMTRY3  36  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY1  37  0.000000  1.000000  0.000000       39.69750
REMARK 290   SMTRY2  37  1.000000  0.000000  0.000000      119.09250
REMARK 290   SMTRY3  37  0.000000  0.000000 -1.000000      119.09250
REMARK 290   SMTRY1  38  0.000000 -1.000000  0.000000       39.69750
REMARK 290   SMTRY2  38 -1.000000  0.000000  0.000000       39.69750
REMARK 290   SMTRY3  38  0.000000  0.000000 -1.000000       39.69750
REMARK 290   SMTRY1  39  0.000000  1.000000  0.000000      119.09250
REMARK 290   SMTRY2  39 -1.000000  0.000000  0.000000      119.09250
REMARK 290   SMTRY3  39  0.000000  0.000000  1.000000       39.69750
REMARK 290   SMTRY1  40  0.000000 -1.000000  0.000000      119.09250
REMARK 290   SMTRY2  40  1.000000  0.000000  0.000000       39.69750
REMARK 290   SMTRY3  40  0.000000  0.000000  1.000000      119.09250
REMARK 290   SMTRY1  41  1.000000  0.000000  0.000000       39.69750
REMARK 290   SMTRY2  41  0.000000  0.000000  1.000000      119.09250
REMARK 290   SMTRY3  41  0.000000 -1.000000  0.000000      119.09250
REMARK 290   SMTRY1  42 -1.000000  0.000000  0.000000      119.09250
REMARK 290   SMTRY2  42  0.000000  0.000000  1.000000       39.69750
REMARK 290   SMTRY3  42  0.000000  1.000000  0.000000      119.09250
REMARK 290   SMTRY1  43 -1.000000  0.000000  0.000000       39.69750
REMARK 290   SMTRY2  43  0.000000  0.000000 -1.000000       39.69750
REMARK 290   SMTRY3  43  0.000000 -1.000000  0.000000       39.69750
REMARK 290   SMTRY1  44  1.000000  0.000000  0.000000      119.09250
REMARK 290   SMTRY2  44  0.000000  0.000000 -1.000000      119.09250
REMARK 290   SMTRY3  44  0.000000  1.000000  0.000000       39.69750
REMARK 290   SMTRY1  45  0.000000  0.000000  1.000000       39.69750
REMARK 290   SMTRY2  45  0.000000  1.000000  0.000000      119.09250
REMARK 290   SMTRY3  45 -1.000000  0.000000  0.000000      119.09250
REMARK 290   SMTRY1  46  0.000000  0.000000  1.000000      119.09250
REMARK 290   SMTRY2  46  0.000000 -1.000000  0.000000      119.09250
REMARK 290   SMTRY3  46  1.000000  0.000000  0.000000       39.69750
REMARK 290   SMTRY1  47  0.000000  0.000000 -1.000000      119.09250
REMARK 290   SMTRY2  47  0.000000  1.000000  0.000000       39.69750
REMARK 290   SMTRY3  47  1.000000  0.000000  0.000000      119.09250
REMARK 290   SMTRY1  48  0.000000  0.000000 -1.000000       39.69750
REMARK 290   SMTRY2  48  0.000000 -1.000000  0.000000       39.69750
REMARK 290   SMTRY3  48 -1.000000  0.000000  0.000000       39.69750
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     MET A    37
REMARK 465     ALA A    38
REMARK 465     ASP A    39
REMARK 465     GLY A   192
REMARK 465     GLN A   193
REMARK 465     ASP A   194
REMARK 465     GLU A   290
REMARK 465     HIS A   291
REMARK 465     HIS A   292
REMARK 465     HIS A   293
REMARK 465     HIS A   294
REMARK 465     HIS A   295
REMARK 465     HIS A   296
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE
REMARK 500   OG   SER A   162     NE2  HIS A   240              1.80
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
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   RES CSSEQI ATM2   DEVIATION
REMARK 500    SER A 162   CA    SER A 162   CB      0.142
REMARK 500    SER A 162   CB    SER A 162   OG      0.130
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3
REMARK 500    ASP A 266   CA  -  CB  -  CG  ANGL. DEV. =  17.8 DEGREES
REMARK 500    ASP A 266   CB  -  CG  -  OD1 ANGL. DEV. =   8.8 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  93       41.57     39.84
REMARK 500    SER A 162     -118.48     42.64
REMARK 500    HIS A 218      -84.58   -122.91
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500  M RES CSSEQI        RMS     TYPE
REMARK 500    ARG A 148         0.13    SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 8YTU   RELATED DB: PDB
REMARK 900 RELATED ID: 8YTV   RELATED DB: PDB
DBREF1 8YTW A   38   288  UNP                  A0A3E0H050_9PSEU
DBREF2 8YTW A     A0A3E0H050                         38         288
SEQADV 8YTW MET A   37  UNP  A0A3E0H05           INITIATING METHIONINE
SEQADV 8YTW LEU A  289  UNP  A0A3E0H05           EXPRESSION TAG
SEQADV 8YTW GLU A  290  UNP  A0A3E0H05           EXPRESSION TAG
SEQADV 8YTW HIS A  291  UNP  A0A3E0H05           EXPRESSION TAG
SEQADV 8YTW HIS A  292  UNP  A0A3E0H05           EXPRESSION TAG
SEQADV 8YTW HIS A  293  UNP  A0A3E0H05           EXPRESSION TAG
SEQADV 8YTW HIS A  294  UNP  A0A3E0H05           EXPRESSION TAG
SEQADV 8YTW HIS A  295  UNP  A0A3E0H05           EXPRESSION TAG
SEQADV 8YTW HIS A  296  UNP  A0A3E0H05           EXPRESSION TAG
SEQRES   1 A  260  MET ALA ASP GLN VAL GLY GLN ALA PRO THR ALA ALA ASN
SEQRES   2 A  260  ILE THR GLY ASP GLY SER PHE ALA THR ALA SER ALA PRO
SEQRES   3 A  260  ILE THR ASN GLN THR GLY PHE GLY GLY GLY THR VAL TYR
SEQRES   4 A  260  TYR PRO THR ALA ALA GLY THR TYR PRO VAL VAL ALA VAL
SEQRES   5 A  260  VAL PRO GLY PHE VAL SER THR TRP SER GLN ILE SER TRP
SEQRES   6 A  260  LEU GLY PRO ARG VAL ALA SER TRP GLY PHE VAL VAL VAL
SEQRES   7 A  260  GLY ALA ASP THR THR SER GLY PHE ASP SER PRO SER GLN
SEQRES   8 A  260  ARG ALA ASP GLU LEU LEU ALA ALA LEU ASN TRP ALA VAL
SEQRES   9 A  260  ASN SER ALA PRO ALA ALA VAL ARG GLY LYS VAL ASP GLY
SEQRES  10 A  260  THR ARG ARG GLY VAL ALA GLY TRP SER MET GLY GLY GLY
SEQRES  11 A  260  GLY THR LEU GLU ALA LEU ALA LYS ASP THR THR GLY THR
SEQRES  12 A  260  VAL LYS ALA GLY VAL PRO LEU ALA PRO TRP ASP ILE GLY
SEQRES  13 A  260  GLN ASP PHE SER LYS VAL THR LYS PRO VAL PHE ILE VAL
SEQRES  14 A  260  GLY ALA GLN ASN ASP THR ILE ALA PRO PRO ALA GLN HIS
SEQRES  15 A  260  ALA VAL PRO PHE TYR ASN ALA ALA ALA GLY PRO LYS SER
SEQRES  16 A  260  TYR LEU GLU LEU ALA GLY ALA ASP HIS PHE PHE PRO THR
SEQRES  17 A  260  THR ALA ASN PRO THR VAL SER ARG ALA MET VAL SER TRP
SEQRES  18 A  260  LEU LYS ARG PHE VAL SER SER ASP ASP ARG PHE THR PRO
SEQRES  19 A  260  PHE THR CYS GLY PHE ALA GLY ALA ALA VAL SER ALA PHE
SEQRES  20 A  260  ARG SER THR ALA CYS LEU GLU HIS HIS HIS HIS HIS HIS
HELIX    1 AA1 THR A   95  SER A  100  5                                   6
HELIX    2 AA2 TRP A  101  SER A  108  1                                   8
HELIX    3 AA3 SER A  124  SER A  142  1                                  19
HELIX    4 AA4 PRO A  144  GLY A  149  1                                   6
HELIX    5 AA5 MET A  163  ASP A  175  1                                  13
HELIX    6 AA6 HIS A  218  ALA A  226  1                                   9
HELIX    7 AA7 PHE A  241  THR A  245  5                                   5
HELIX    8 AA8 ASN A  247  VAL A  262  1                                  16
HELIX    9 AA9 ASP A  265  CYS A  273  5                                   9
SHEET    1 AA1 6 THR A  58  PRO A  62  0
SHEET    2 AA1 6 GLY A  71  PRO A  77 -1  O  TYR A  76   N  ALA A  59
SHEET    3 AA1 6 VAL A 112  ASP A 117 -1  O  GLY A 115   N  THR A  73
SHEET    4 AA1 6 TYR A  83  VAL A  89  1  N  VAL A  86   O  VAL A 112
SHEET    5 AA1 6 VAL A 151  SER A 162  1  O  ASP A 152   N  TYR A  83
SHEET    6 AA1 6 VAL A 180  PRO A 188  1  O  LEU A 186   N  GLY A 160
SHEET    1 AA2 3 VAL A 202  ALA A 207  0
SHEET    2 AA2 3 LYS A 230  LEU A 235  1  O  SER A 231   N  ILE A 204
SHEET    3 AA2 3 VAL A 280  SER A 285 -1  O  ARG A 284   N  TYR A 232
SSBOND   1 CYS A  273    CYS A  288                          1555   1555  2.40
CRYST1  158.790  158.790  158.790  90.00  90.00  90.00 I 41 3 2     48
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      0.006298  0.000000  0.000000        0.00000
SCALE2      0.000000  0.006298  0.000000        0.00000
SCALE3      0.000000  0.000000  0.006298        0.00000
TER    1794      LEU A 289
MASTER      520    0    0    9    9    0    0    6 1793    1    2   20
END