longtext: 3WIO-pdb

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HEADER    HYDROLASE                               22-SEP-13   3WIO
TITLE     CRYSTAL STRUCTURE OF OSD14 IN COMPLEX WITH HYDROXY D-RING
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: PROBABLE STRIGOLACTONE ESTERASE D14;
COMPND   3 CHAIN: A, B;
COMPND   4 FRAGMENT: UNP RESIDUES 54-318;
COMPND   5 SYNONYM: DWARF 88 ESTERASE, PROTEIN DWARF-14, PROTEIN DWARF-88,
COMPND   6 PROTEIN HIGH-TILLERING DWARF 2;
COMPND   7 EC: 3.1.-.-;
COMPND   8 ENGINEERED: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: ORYZA SATIVA JAPONICA GROUP;
SOURCE   3 ORGANISM_COMMON: JAPONICA RICE;
SOURCE   4 ORGANISM_TAXID: 39947;
SOURCE   5 GENE: D14, D88, HTD2, LOC_OS03G10620, OS03G0203200;
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID
KEYWDS    ALPHA/BETA-HYDROLASE FOLD, HYDROLASE
EXPDTA    X-RAY DIFFRACTION
AUTHOR    Y.-L.XUE,T.MIYAKAWA,F.HOU,H.-M.QIN,M.TANOKURA
REVDAT   1   23-OCT-13 3WIO    0
JRNL        AUTH   H.NAKAMURA,Y.-L.XUE,T.MIYAKAWA,F.HOU,H.-M.QIN,K.FUKUI,X.SHI,
JRNL        AUTH 2 E.ITO,S.ITO,S.-H.PARK,Y.MIYAUCHI,A.ASANO,N.TOTSUKA,T.UEDA,
JRNL        AUTH 3 M.TANOKURA,T.ASAMI
JRNL        TITL   MOLECULAR MECHANISM OF STRIGOLACTONE PERCEPTION BY DWARF14
JRNL        REF    NAT COMMUN                                 2013
JRNL        REFN                   ESSN 2041-1723
JRNL        DOI    10.1038/NCOMMS3613
REMARK   2
REMARK   2 RESOLUTION.    2.10 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : REFMAC 5.5.0109
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON
REMARK   3
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.10
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 20.00
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL
REMARK   3   COMPLETENESS FOR RANGE        (%) : 100.0
REMARK   3   NUMBER OF REFLECTIONS             : 28858
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) : 0.191
REMARK   3   R VALUE            (WORKING SET) : 0.188
REMARK   3   FREE R VALUE                     : 0.246
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100
REMARK   3   FREE R VALUE TEST SET COUNT      : 1537
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) : 2.10
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.15
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2047
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 100.00
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2110
REMARK   3   BIN FREE R VALUE SET COUNT          : 96
REMARK   3   BIN FREE R VALUE                    : 0.2980
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 4108
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 8
REMARK   3   SOLVENT ATOMS            : 195
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : NULL
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 22.01
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : 0.49000
REMARK   3    B22 (A**2) : -0.54000
REMARK   3    B33 (A**2) : 0.05000
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): 0.245
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.203
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.141
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 5.279
REMARK   3
REMARK   3 CORRELATION COEFFICIENTS.
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.941
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.904
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  4206 ; 0.022 ; 0.022
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  5729 ; 1.879 ; 1.960
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   529 ; 6.307 ; 5.000
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   186 ;29.963 ;22.043
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   653 ;17.731 ;15.000
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    42 ;20.751 ;15.000
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   664 ; 0.128 ; 0.200
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  3218 ; 0.009 ; 0.021
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL
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):  2643 ; 1.050 ; 1.500
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  4254 ; 1.865 ; 2.000
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1563 ; 3.130 ; 3.000
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1475 ; 4.764 ; 4.500
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL
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   : 1.40
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 3WIO COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 02-OCT-13.
REMARK 100 THE RCSB ID CODE IS RCSB096383.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 30-MAR-12
REMARK 200  TEMPERATURE           (KELVIN) : 77
REMARK 200  PH                             : 7.5
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 FR-E SUPERBRIGHT
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 RAXIS VII
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200  DATA SCALING SOFTWARE          : XSCALE
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 30394
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.100
REMARK 200  RESOLUTION RANGE LOW       (A) : 20.000
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : NULL
REMARK 200  DATA REDUNDANCY                : 7.100
REMARK 200  R MERGE                    (I) : NULL
REMARK 200  R SYM                      (I) : 0.08600
REMARK 200   FOR THE DATA SET  : 20.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.10
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.15
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL
REMARK 200  DATA REDUNDANCY IN SHELL       : 7.00
REMARK 200  R MERGE FOR SHELL          (I) : NULL
REMARK 200  R SYM FOR SHELL            (I) : 0.43000
REMARK 200   FOR SHELL         : 5.200
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: 3VXK
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 41.78
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.11
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 8% PEG 20000, 2% 1,4-DIOXANE, 0.1M
REMARK 280  HEPES, PH 7.5, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 277K
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       24.19000
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       59.51000
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       44.06500
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       59.51000
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       24.19000
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       44.06500
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465   M RES C SSSEQI
REMARK 465     GLY A    45
REMARK 465     PRO A    46
REMARK 465     GLY A    47
REMARK 465     TYR A    48
REMARK 465     GLN A    49
REMARK 465     ASP A    50
REMARK 465     PRO A    51
REMARK 465     ASN A    52
REMARK 465     SER A    53
REMARK 465     GLY B    45
REMARK 465     PRO B    46
REMARK 465     GLY B    47
REMARK 465     TYR B    48
REMARK 465     GLN B    49
REMARK 465     ASP B    50
REMARK 465     PRO B    51
REMARK 465     ASN B    52
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 B   162     O    HOH B   455              2.15
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    CYS B 241   CB    CYS B 241   SG     -0.116
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 196   CB  -  CG  -  OD1 ANGL. DEV. =   5.9 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    SER A  67      149.17   -170.97
REMARK 500    TYR A 119       42.80    -87.21
REMARK 500    SER A 147     -128.93     68.36
REMARK 500    ARG A 175      128.17   -173.00
REMARK 500    SER A 180      -65.44    -27.84
REMARK 500    ASN A 201       89.71   -153.83
REMARK 500    GLN A 293       23.28    -79.85
REMARK 500    ASP B  81     -164.64   -123.20
REMARK 500    ARG B 117      -61.21    -90.39
REMARK 500    SER B 147     -110.21     48.27
REMARK 500    ASP B 179       82.50   -170.02
REMARK 500    SER B 180     -140.31     58.36
REMARK 500    ASN B 201       82.03   -152.81
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE H3M A 401
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3VXK   RELATED DB: PDB
DBREF  3WIO A   54   318  UNP    Q10QA5   D14_ORYSJ       54    318
DBREF  3WIO B   54   318  UNP    Q10QA5   D14_ORYSJ       54    318
SEQADV 3WIO GLY A   45  UNP  Q10QA5              EXPRESSION TAG
SEQADV 3WIO PRO A   46  UNP  Q10QA5              EXPRESSION TAG
SEQADV 3WIO GLY A   47  UNP  Q10QA5              EXPRESSION TAG
SEQADV 3WIO TYR A   48  UNP  Q10QA5              EXPRESSION TAG
SEQADV 3WIO GLN A   49  UNP  Q10QA5              EXPRESSION TAG
SEQADV 3WIO ASP A   50  UNP  Q10QA5              EXPRESSION TAG
SEQADV 3WIO PRO A   51  UNP  Q10QA5              EXPRESSION TAG
SEQADV 3WIO ASN A   52  UNP  Q10QA5              EXPRESSION TAG
SEQADV 3WIO SER A   53  UNP  Q10QA5              EXPRESSION TAG
SEQADV 3WIO GLY B   45  UNP  Q10QA5              EXPRESSION TAG
SEQADV 3WIO PRO B   46  UNP  Q10QA5              EXPRESSION TAG
SEQADV 3WIO GLY B   47  UNP  Q10QA5              EXPRESSION TAG
SEQADV 3WIO TYR B   48  UNP  Q10QA5              EXPRESSION TAG
SEQADV 3WIO GLN B   49  UNP  Q10QA5              EXPRESSION TAG
SEQADV 3WIO ASP B   50  UNP  Q10QA5              EXPRESSION TAG
SEQADV 3WIO PRO B   51  UNP  Q10QA5              EXPRESSION TAG
SEQADV 3WIO ASN B   52  UNP  Q10QA5              EXPRESSION TAG
SEQADV 3WIO SER B   53  UNP  Q10QA5              EXPRESSION TAG
SEQRES   1 A  274  GLY PRO GLY TYR GLN ASP PRO ASN SER ALA LYS LEU LEU
SEQRES   2 A  274  GLN ILE LEU ASN VAL ARG VAL VAL GLY SER GLY GLU ARG
SEQRES   3 A  274  VAL VAL VAL LEU SER HIS GLY PHE GLY THR ASP GLN SER
SEQRES   4 A  274  ALA TRP SER ARG VAL LEU PRO TYR LEU THR ARG ASP HIS
SEQRES   5 A  274  ARG VAL VAL LEU TYR ASP LEU VAL CYS ALA GLY SER VAL
SEQRES   6 A  274  ASN PRO ASP HIS PHE ASP PHE ARG ARG TYR ASP ASN LEU
SEQRES   7 A  274  ASP ALA TYR VAL ASP ASP LEU LEU ALA ILE LEU ASP ALA
SEQRES   8 A  274  LEU ARG ILE PRO ARG CYS ALA PHE VAL GLY HIS SER VAL
SEQRES   9 A  274  SER ALA MET ILE GLY ILE LEU ALA SER ILE ARG ARG PRO
SEQRES  10 A  274  ASP LEU PHE ALA LYS LEU VAL LEU ILE GLY ALA SER PRO
SEQRES  11 A  274  ARG PHE LEU ASN ASP SER ASP TYR HIS GLY GLY PHE GLU
SEQRES  12 A  274  LEU GLU GLU ILE GLN GLN VAL PHE ASP ALA MET GLY ALA
SEQRES  13 A  274  ASN TYR SER ALA TRP ALA THR GLY TYR ALA PRO LEU ALA
SEQRES  14 A  274  VAL GLY ALA ASP VAL PRO ALA ALA VAL GLN GLU PHE SER
SEQRES  15 A  274  ARG THR LEU PHE ASN MET ARG PRO ASP ILE SER LEU HIS
SEQRES  16 A  274  VAL CYS GLN THR VAL PHE LYS THR ASP LEU ARG GLY VAL
SEQRES  17 A  274  LEU GLY MET VAL ARG ALA PRO CYS VAL VAL VAL GLN THR
SEQRES  18 A  274  THR ARG ASP VAL SER VAL PRO ALA SER VAL ALA ALA TYR
SEQRES  19 A  274  LEU LYS ALA HIS LEU GLY GLY ARG THR THR VAL GLU PHE
SEQRES  20 A  274  LEU GLN THR GLU GLY HIS LEU PRO HIS LEU SER ALA PRO
SEQRES  21 A  274  SER LEU LEU ALA GLN VAL LEU ARG ARG ALA LEU ALA ARG
SEQRES  22 A  274  TYR
SEQRES   1 B  274  GLY PRO GLY TYR GLN ASP PRO ASN SER ALA LYS LEU LEU
SEQRES   2 B  274  GLN ILE LEU ASN VAL ARG VAL VAL GLY SER GLY GLU ARG
SEQRES   3 B  274  VAL VAL VAL LEU SER HIS GLY PHE GLY THR ASP GLN SER
SEQRES   4 B  274  ALA TRP SER ARG VAL LEU PRO TYR LEU THR ARG ASP HIS
SEQRES   5 B  274  ARG VAL VAL LEU TYR ASP LEU VAL CYS ALA GLY SER VAL
SEQRES   6 B  274  ASN PRO ASP HIS PHE ASP PHE ARG ARG TYR ASP ASN LEU
SEQRES   7 B  274  ASP ALA TYR VAL ASP ASP LEU LEU ALA ILE LEU ASP ALA
SEQRES   8 B  274  LEU ARG ILE PRO ARG CYS ALA PHE VAL GLY HIS SER VAL
SEQRES   9 B  274  SER ALA MET ILE GLY ILE LEU ALA SER ILE ARG ARG PRO
SEQRES  10 B  274  ASP LEU PHE ALA LYS LEU VAL LEU ILE GLY ALA SER PRO
SEQRES  11 B  274  ARG PHE LEU ASN ASP SER ASP TYR HIS GLY GLY PHE GLU
SEQRES  12 B  274  LEU GLU GLU ILE GLN GLN VAL PHE ASP ALA MET GLY ALA
SEQRES  13 B  274  ASN TYR SER ALA TRP ALA THR GLY TYR ALA PRO LEU ALA
SEQRES  14 B  274  VAL GLY ALA ASP VAL PRO ALA ALA VAL GLN GLU PHE SER
SEQRES  15 B  274  ARG THR LEU PHE ASN MET ARG PRO ASP ILE SER LEU HIS
SEQRES  16 B  274  VAL CYS GLN THR VAL PHE LYS THR ASP LEU ARG GLY VAL
SEQRES  17 B  274  LEU GLY MET VAL ARG ALA PRO CYS VAL VAL VAL GLN THR
SEQRES  18 B  274  THR ARG ASP VAL SER VAL PRO ALA SER VAL ALA ALA TYR
SEQRES  19 B  274  LEU LYS ALA HIS LEU GLY GLY ARG THR THR VAL GLU PHE
SEQRES  20 B  274  LEU GLN THR GLU GLY HIS LEU PRO HIS LEU SER ALA PRO
SEQRES  21 B  274  SER LEU LEU ALA GLN VAL LEU ARG ARG ALA LEU ALA ARG
SEQRES  22 B  274  TYR
HET    H3M  A 401       8
HETNAM     H3M (5R)-5-HYDROXY-3-METHYLFURAN-2(5H)-ONE
FORMUL   3  H3M    C5 H6 O3
FORMUL   4  HOH   *195(H2 O)
HELIX    1   1 ALA A   54  LEU A   60  1                                   7
HELIX    2   2 ASP A   81  SER A   86  5                                   6
HELIX    3   3 VAL A   88  LEU A   92  5                                   5
HELIX    4   4 ASN A  110  PHE A  114  5                                   5
HELIX    5   5 ARG A  117  ASN A  121  5                                   5
HELIX    6   6 LEU A  122  ARG A  137  1                                  16
HELIX    7   7 SER A  147  ARG A  160  1                                  14
HELIX    8   8 GLU A  187  ASN A  201  1                                  15
HELIX    9   9 ASN A  201  GLY A  215  1                                  15
HELIX   10  10 VAL A  218  MET A  232  1                                  15
HELIX   11  11 ARG A  233  LYS A  246  1                                  14
HELIX   12  12 LEU A  249  VAL A  256  5                                   8
HELIX   13  13 SER A  274  LEU A  283  1                                  10
HELIX   14  14 LEU A  298  ALA A  303  1                                   6
HELIX   15  15 ALA A  303  LEU A  315  1                                  13
HELIX   16  16 LYS B   55  LEU B   60  1                                   6
HELIX   17  17 ASP B   81  SER B   86  5                                   6
HELIX   18  18 LEU B   89  ARG B   94  1                                   6
HELIX   19  19 ASN B  110  PHE B  114  5                                   5
HELIX   20  20 ARG B  117  ASP B  120  5                                   4
HELIX   21  21 ASN B  121  LEU B  136  1                                  16
HELIX   22  22 SER B  147  ARG B  160  1                                  14
HELIX   23  23 GLU B  187  ASN B  201  1                                  15
HELIX   24  24 ASN B  201  GLY B  215  1                                  15
HELIX   25  25 VAL B  218  MET B  232  1                                  15
HELIX   26  26 ARG B  233  LYS B  246  1                                  14
HELIX   27  27 LEU B  249  VAL B  256  5                                   8
HELIX   28  28 SER B  274  LEU B  283  1                                  10
HELIX   29  29 LEU B  298  ALA B  303  1                                   6
HELIX   30  30 ALA B  303  ARG B  317  1                                  15
SHEET    1   A 7 ARG A  63  GLY A  66  0
SHEET    2   A 7 ARG A  97  LEU A 100 -1  O  VAL A  98   N  VAL A  65
SHEET    3   A 7 VAL A  71  SER A  75  1  N  VAL A  72   O  VAL A  99
SHEET    4   A 7 CYS A 141  HIS A 146  1  O  VAL A 144   N  SER A  75
SHEET    5   A 7 PHE A 164  ILE A 170  1  O  ILE A 170   N  GLY A 145
SHEET    6   A 7 CYS A 260  GLN A 264  1  O  VAL A 261   N  LEU A 169
SHEET    7   A 7 THR A 287  PHE A 291  1  O  THR A 288   N  VAL A 262
SHEET    1   B 7 ARG B  63  GLY B  66  0
SHEET    2   B 7 ARG B  97  LEU B 100 -1  O  VAL B  98   N  VAL B  65
SHEET    3   B 7 VAL B  71  SER B  75  1  N  LEU B  74   O  VAL B  99
SHEET    4   B 7 CYS B 141  HIS B 146  1  O  VAL B 144   N  SER B  75
SHEET    5   B 7 PHE B 164  ILE B 170  1  O  ALA B 165   N  CYS B 141
SHEET    6   B 7 CYS B 260  GLN B 264  1  O  VAL B 261   N  LEU B 169
SHEET    7   B 7 THR B 287  PHE B 291  1  O  GLU B 290   N  GLN B 264
SITE     1 AC1  6 PHE A 186  VAL A 194  TRP A 205  TYR A 209
SITE     2 AC1  6 PHE A 245  SER A 270
CRYST1   48.380   88.130  119.020  90.00  90.00  90.00 P 21 21 21    8
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      0.020670  0.000000  0.000000        0.00000
SCALE2      0.000000  0.011347  0.000000        0.00000
SCALE3      0.000000  0.000000  0.008402        0.00000
TER    2052      TYR A 318
TER    4110      TYR B 318
MASTER      354    0    1   30   14    0    2    6 4311    2    8   44
END