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PDBsum entry 1cgk

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Transferase PDB id
1cgk
Jmol
Contents
Protein chain
387 a.a. *
Ligands
NAR
Waters ×360
* Residue conservation analysis
HEADER    TRANSFERASE                             25-MAR-99   1CGK
TITLE     CHALCONE SYNTHASE FROM ALFALFA COMPLEXED WITH NARINGENIN
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: PROTEIN (CHALCONE SYNTHASE);
COMPND   3 CHAIN: A;
COMPND   4 SYNONYM: CHS;
COMPND   5 EC: 2.3.1.74;
COMPND   6 ENGINEERED: YES;
COMPND   7 OTHER_DETAILS: COMPLEXED WITH NARINGENIN
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: MEDICAGO SATIVA;
SOURCE   3 ORGANISM_TAXID: 3879;
SOURCE   4 TISSUE: 21 DAY OLD ROOT NODULE;
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21;
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE   8 EXPRESSION_SYSTEM_PLASMID: PET28B
KEYWDS    POLYKETIDE SYNTHASE, CHALCONE BIOSYNTHESIS, TRANSFERASE
EXPDTA    X-RAY DIFFRACTION
AUTHOR    J.-L.FERRER,J.JEZ,M.E.BOWMAN,R.DIXON,J.P.NOEL
REVDAT   5   13-JUL-11 1CGK    1       VERSN
REVDAT   4   24-FEB-09 1CGK    1       VERSN
REVDAT   3   01-APR-03 1CGK    1       JRNL
REVDAT   2   05-OCT-99 1CGK    1       JRNL
REVDAT   1   03-SEP-99 1CGK    0
JRNL        AUTH   J.L.FERRER,J.M.JEZ,M.E.BOWMAN,R.A.DIXON,J.P.NOEL
JRNL        TITL   STRUCTURE OF CHALCONE SYNTHASE AND THE MOLECULAR BASIS OF
JRNL        TITL 2 PLANT POLYKETIDE BIOSYNTHESIS.
JRNL        REF    NAT.STRUCT.BIOL.              V.   6   775 1999
JRNL        REFN                   ISSN 1072-8368
JRNL        PMID   10426957
JRNL        DOI    10.1038/11553
REMARK   2
REMARK   2 RESOLUTION.    1.84 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : REFMAC
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.84
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 84.50
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000
REMARK   3   COMPLETENESS FOR RANGE        (%) : 85.5
REMARK   3   NUMBER OF REFLECTIONS             : 26948
REMARK   3
REMARK   3  FIT TO DATA USED IN REFINEMENT.
REMARK   3   CROSS-VALIDATION METHOD          : NULL
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM
REMARK   3   R VALUE     (WORKING + TEST SET) : NULL
REMARK   3   R VALUE            (WORKING SET) : 0.161
REMARK   3   FREE R VALUE                     : 0.225
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000
REMARK   3   FREE R VALUE TEST SET COUNT      : 1347
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 2980
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 20
REMARK   3   SOLVENT ATOMS            : 360
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : NULL
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : NULL
REMARK   3    B22 (A**2) : NULL
REMARK   3    B33 (A**2) : NULL
REMARK   3    B12 (A**2) : NULL
REMARK   3    B13 (A**2) : NULL
REMARK   3    B23 (A**2) : NULL
REMARK   3
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.
REMARK   3   ESU BASED ON R VALUE                            (A): NULL
REMARK   3   ESU BASED ON FREE R VALUE                       (A): NULL
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): NULL
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): NULL
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.
REMARK   3   DISTANCE RESTRAINTS.                    RMS    SIGMA
REMARK   3    BOND LENGTH                     (A) : 0.013 ; NULL
REMARK   3    ANGLE DISTANCE                  (A) : 2.419 ; NULL
REMARK   3    INTRAPLANAR 1-4 DISTANCE        (A) : NULL  ; NULL
REMARK   3    H-BOND OR METAL COORDINATION    (A) : NULL  ; NULL
REMARK   3
REMARK   3   PLANE RESTRAINT                  (A) : NULL  ; NULL
REMARK   3   CHIRAL-CENTER RESTRAINT       (A**3) : NULL  ; NULL
REMARK   3
REMARK   3   NON-BONDED CONTACT RESTRAINTS.
REMARK   3    SINGLE TORSION                  (A) : NULL  ; NULL
REMARK   3    MULTIPLE TORSION                (A) : NULL  ; NULL
REMARK   3    H-BOND (X...Y)                  (A) : NULL  ; NULL
REMARK   3    H-BOND (X-H...Y)                (A) : NULL  ; NULL
REMARK   3
REMARK   3   CONFORMATIONAL TORSION ANGLE RESTRAINTS.
REMARK   3    SPECIFIED                 (DEGREES) : NULL  ; NULL
REMARK   3    PLANAR                    (DEGREES) : NULL  ; NULL
REMARK   3    STAGGERED                 (DEGREES) : NULL  ; NULL
REMARK   3    TRANSVERSE                (DEGREES) : NULL  ; NULL
REMARK   3
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA
REMARK   3   MAIN-CHAIN BOND              (A**2) : NULL  ; NULL
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: NULL
REMARK   4
REMARK   4 1CGK COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 24-MAR-99.
REMARK 100 THE RCSB ID CODE IS RCSB000721.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : JUN-98
REMARK 200  TEMPERATURE           (KELVIN) : 105.0
REMARK 200  PH                             : 6.50
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          : MACSCIENCE SRA
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418
REMARK 200  MONOCHROMATOR                  : NI FILTER
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE
REMARK 200  DETECTOR MANUFACTURER          : MAC SCIENCE DIP-2000
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 26948
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.840
REMARK 200  RESOLUTION RANGE LOW       (A) : 51.680
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 86.6
REMARK 200  DATA REDUNDANCY                : 2.800
REMARK 200  R MERGE                    (I) : NULL
REMARK 200  R SYM                      (I) : 0.04100
REMARK 200   FOR THE DATA SET  : 13.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.84
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.89
REMARK 200  COMPLETENESS FOR SHELL     (%) : 8.3
REMARK 200  DATA REDUNDANCY IN SHELL       : 0.10
REMARK 200  R MERGE FOR SHELL          (I) : NULL
REMARK 200  R SYM FOR SHELL            (I) : 0.01100
REMARK 200   FOR SHELL         : 7.500
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: OTHER
REMARK 200 SOFTWARE USED: CCP4 (ARPP)
REMARK 200 STARTING MODEL: PDB ENTRY 1BI5
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 42.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.07
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: THE DROPLE CONSISTED ON 25 MGR/ML
REMARK 280  (FINAL CONCENTRATION) PROTEIN MIXED WITH THE RESERVOIR WHICH
REMARK 280  CONTAINED 2.4 M AMMONIUM SULFATE, 100 MM PIPES BUFFER (PH 6.5) ,
REMARK 280  IN THE PRESENCE (UP TO 5 MM) OR ABSENCE OF DTT REDUCING AGENT.
REMARK 280  CRYSTALS WERE STABILIZED IN 40% (V/V) PEG400, 100 MM PIPES 16 MM
REMARK 280  NARINGENIN PRIOR TO FREEZING AT 105 K, PH 6.50
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32 2 1
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -Y,X-Y,Z+2/3
REMARK 290       3555   -X+Y,-X,Z+1/3
REMARK 290       4555   Y,X,-Z
REMARK 290       5555   X-Y,-Y,-Z+1/3
REMARK 290       6555   -X,-X+Y,-Z+2/3
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 -0.500000 -0.866025  0.000000        0.00000
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       43.45733
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       21.72867
REMARK 290   SMTRY1   4 -0.500000  0.866025  0.000000        0.00000
REMARK 290   SMTRY2   4  0.866025  0.500000  0.000000        0.00000
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   5  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000       21.72867
REMARK 290   SMTRY1   6 -0.500000 -0.866025  0.000000        0.00000
REMARK 290   SMTRY2   6 -0.866025  0.500000  0.000000        0.00000
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000       43.45733
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA,PQS
REMARK 350 TOTAL BURIED SURFACE AREA: 7330 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 26390 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -12.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000
REMARK 350   BIOMT1   2 -0.500000  0.866025  0.000000        0.00000
REMARK 350   BIOMT2   2  0.866025  0.500000  0.000000        0.00000
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000      130.37200
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      HOH A 415  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     MET A     1
REMARK 465     VAL A     2
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE
REMARK 500   CG   LYS A     9     O    HOH A   693     4557     1.82
REMARK 500   NZ   LYS A   146     OE2  GLU A   251     4557     1.86
REMARK 500   O    HOH A   668     O    HOH A   715     4557     1.99
REMARK 500   O    HOH A   596     O    HOH A   626     4557     2.02
REMARK 500   NZ   LYS A   155     O    HOH A   556     4557     2.13
REMARK 500   O    HOH A   409     O    HOH A   441     4557     2.15
REMARK 500   O    HOH A   462     O    HOH A   474     5666     2.15
REMARK 500   O    HOH A   459     O    HOH A   660     4556     2.16
REMARK 500   N    MET A   158     O    HOH A   435     4557     2.19
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    ARG A  12   NE  -  CZ  -  NH1 ANGL. DEV. =  -4.2 DEGREES
REMARK 500    ASP A  38   CB  -  CG  -  OD1 ANGL. DEV. =   6.7 DEGREES
REMARK 500    ARG A  67   CD  -  NE  -  CZ  ANGL. DEV. =  23.9 DEGREES
REMARK 500    ARG A  67   NE  -  CZ  -  NH1 ANGL. DEV. =   6.5 DEGREES
REMARK 500    ASP A 136   CB  -  CG  -  OD1 ANGL. DEV. =   6.1 DEGREES
REMARK 500    PRO A 138   N   -  CA  -  CB  ANGL. DEV. =   8.2 DEGREES
REMARK 500    ARG A 156   NE  -  CZ  -  NH2 ANGL. DEV. =   3.9 DEGREES
REMARK 500    ARG A 172   NE  -  CZ  -  NH1 ANGL. DEV. =   3.4 DEGREES
REMARK 500    VAL A 342   CB  -  CA  -  C   ANGL. DEV. =  12.2 DEGREES
REMARK 500    VAL A 342   N   -  CA  -  CB  ANGL. DEV. = -17.1 DEGREES
REMARK 500    VAL A 342   CA  -  CB  -  CG1 ANGL. DEV. =  10.0 DEGREES
REMARK 500    GLY A 376   CA  -  C   -  N   ANGL. DEV. =  19.5 DEGREES
REMARK 500    GLY A 376   O   -  C   -  N   ANGL. DEV. = -14.8 DEGREES
REMARK 500    ILE A 389   CA  -  CB  -  CG2 ANGL. DEV. =  12.3 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  90       -0.06   -159.17
REMARK 500    GLU A 231       15.66     55.31
REMARK 500    TYR A 334      -14.78   -140.67
REMARK 500    MET A 337       33.54    -96.36
REMARK 500    SER A 338     -132.15     47.04
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY
REMARK 500
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 500 I=INSERTION CODE).
REMARK 500
REMARK 500  M RES CSSEQI        ANGLE
REMARK 500    GLU A  32        -18.07
REMARK 500    LYS A  42        -14.77
REMARK 500    GLU A 333         12.42
REMARK 500    THR A 354        -18.48
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 689        DISTANCE =  6.04 ANGSTROMS
REMARK 525    HOH A 710        DISTANCE =  7.10 ANGSTROMS
REMARK 525    HOH A 718        DISTANCE =  5.40 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: CYS
REMARK 800 EVIDENCE_CODE: AUTHOR
REMARK 800 SITE_DESCRIPTION: CATALYTIC SITE
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAR A 390
DBREF  1CGK A    1   389  UNP    P30074   CHS2_MEDSA       1    389
SEQRES   1 A  389  MET VAL SER VAL SER GLU ILE ARG LYS ALA GLN ARG ALA
SEQRES   2 A  389  GLU GLY PRO ALA THR ILE LEU ALA ILE GLY THR ALA ASN
SEQRES   3 A  389  PRO ALA ASN CYS VAL GLU GLN SER THR TYR PRO ASP PHE
SEQRES   4 A  389  TYR PHE LYS ILE THR ASN SER GLU HIS LYS THR GLU LEU
SEQRES   5 A  389  LYS GLU LYS PHE GLN ARG MET CYS ASP LYS SER MET ILE
SEQRES   6 A  389  LYS ARG ARG TYR MET TYR LEU THR GLU GLU ILE LEU LYS
SEQRES   7 A  389  GLU ASN PRO ASN VAL CYS GLU TYR MET ALA PRO SER LEU
SEQRES   8 A  389  ASP ALA ARG GLN ASP MET VAL VAL VAL GLU VAL PRO ARG
SEQRES   9 A  389  LEU GLY LYS GLU ALA ALA VAL LYS ALA ILE LYS GLU TRP
SEQRES  10 A  389  GLY GLN PRO LYS SER LYS ILE THR HIS LEU ILE VAL CYS
SEQRES  11 A  389  THR THR SER GLY VAL ASP MET PRO GLY ALA ASP TYR GLN
SEQRES  12 A  389  LEU THR LYS LEU LEU GLY LEU ARG PRO TYR VAL LYS ARG
SEQRES  13 A  389  TYR MET MET TYR GLN GLN GLY CYS PHE ALA GLY GLY THR
SEQRES  14 A  389  VAL LEU ARG LEU ALA LYS ASP LEU ALA GLU ASN ASN LYS
SEQRES  15 A  389  GLY ALA ARG VAL LEU VAL VAL CYS SER GLU VAL THR ALA
SEQRES  16 A  389  VAL THR PHE ARG GLY PRO SER ASP THR HIS LEU ASP SER
SEQRES  17 A  389  LEU VAL GLY GLN ALA LEU PHE GLY ASP GLY ALA ALA ALA
SEQRES  18 A  389  LEU ILE VAL GLY SER ASP PRO VAL PRO GLU ILE GLU LYS
SEQRES  19 A  389  PRO ILE PHE GLU MET VAL TRP THR ALA GLN THR ILE ALA
SEQRES  20 A  389  PRO ASP SER GLU GLY ALA ILE ASP GLY HIS LEU ARG GLU
SEQRES  21 A  389  ALA GLY LEU THR PHE HIS LEU LEU LYS ASP VAL PRO GLY
SEQRES  22 A  389  ILE VAL SER LYS ASN ILE THR LYS ALA LEU VAL GLU ALA
SEQRES  23 A  389  PHE GLU PRO LEU GLY ILE SER ASP TYR ASN SER ILE PHE
SEQRES  24 A  389  TRP ILE ALA HIS PRO GLY GLY PRO ALA ILE LEU ASP GLN
SEQRES  25 A  389  VAL GLU GLN LYS LEU ALA LEU LYS PRO GLU LYS MET ASN
SEQRES  26 A  389  ALA THR ARG GLU VAL LEU SER GLU TYR GLY ASN MET SER
SEQRES  27 A  389  SER ALA CYS VAL LEU PHE ILE LEU ASP GLU MET ARG LYS
SEQRES  28 A  389  LYS SER THR GLN ASN GLY LEU LYS THR THR GLY GLU GLY
SEQRES  29 A  389  LEU GLU TRP GLY VAL LEU PHE GLY PHE GLY PRO GLY LEU
SEQRES  30 A  389  THR ILE GLU THR VAL VAL LEU ARG SER VAL ALA ILE
HET    NAR  A 390      20
HETNAM     NAR NARINGENIN
FORMUL   2  NAR    C15 H12 O5
FORMUL   3  HOH   *360(H2 O)
HELIX    1   1 VAL A    4  GLN A   11  1                                   8
HELIX    2   2 TYR A   36  ILE A   43  1                                   8
HELIX    3   3 THR A   50  LYS A   62  1                                  13
HELIX    4   4 GLU A   74  GLU A   79  1                                   6
HELIX    5   5 PRO A   81  CYS A   84  1                                   4
HELIX    6   6 LEU A   91  TRP A  117  1                                  27
HELIX    7   7 LYS A  121  LYS A  123  5                                   3
HELIX    8   8 ALA A  140  LEU A  148  1                                   9
HELIX    9   9 CYS A  164  GLU A  179  5                                  16
HELIX   10  10 THR A  194  VAL A  196  5                                   3
HELIX   11  11 LEU A  206  LEU A  214  1                                   9
HELIX   12  12 VAL A  271  LEU A  290  1                                  20
HELIX   13  13 PRO A  307  LEU A  317  1                                  11
HELIX   14  14 PRO A  321  TYR A  334  5                                  14
HELIX   15  15 SER A  338  GLN A  355  5                                  18
SHEET    1   A 2 CYS A  30  GLU A  32  0
SHEET    2   A 2 ARG A  67  TYR A  69 -1  N  ARG A  68   O  VAL A  31
SHEET    1   B 5 LYS A 155  TYR A 160  0
SHEET    2   B 5 HIS A 126  THR A 131  1  N  LEU A 127   O  LYS A 155
SHEET    3   B 5 VAL A 186  GLU A 192  1  N  LEU A 187   O  HIS A 126
SHEET    4   B 5 GLY A 218  GLY A 225 -1  N  VAL A 224   O  VAL A 186
SHEET    5   B 5 THR A  18  ALA A  25 -1  N  ALA A  25   O  ALA A 219
SHEET    1   C 4 PHE A 299  ALA A 302  0
SHEET    2   C 4 TRP A 367  GLY A 374  1  N  VAL A 369   O  PHE A 299
SHEET    3   C 4 THR A 378  SER A 386 -1  N  LEU A 384   O  GLY A 368
SHEET    4   C 4 PHE A 237  ILE A 246 -1  N  THR A 245   O  ILE A 379
CISPEP   1 MET A  137    PRO A  138          0       -13.49
CISPEP   2 GLY A  376    LEU A  377          0         5.32
SITE     1 CYS  1 CYS A 164
SITE     1 AC1 18 SER A 133  MET A 137  CYS A 164  GLU A 192
SITE     2 AC1 18 VAL A 193  THR A 194  THR A 197  PHE A 215
SITE     3 AC1 18 GLY A 216  ASP A 217  ILE A 254  ASP A 255
SITE     4 AC1 18 GLY A 256  LEU A 263  THR A 264  PHE A 265
SITE     5 AC1 18 SER A 338  PRO A 375
CRYST1   97.917   97.917   65.186  90.00  90.00 120.00 P 32 2 1      6
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      0.010213  0.005896  0.000000        0.00000
SCALE2      0.000000  0.011793  0.000000        0.00000
SCALE3      0.000000  0.000000  0.015341        0.00000
      
PROCHECK
Go to PROCHECK summary
 References