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PDBsum entry 1cml

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Transferase PDB id
1cml
Jmol
Contents
Protein chain
389 a.a. *
Ligands
SO4
MLC-PIN
Waters ×399
* Residue conservation analysis
HEADER    TRANSFERASE                             30-MAR-99   1CML
TITLE     CHALCONE SYNTHASE FROM ALFALFA COMPLEXED WITH MALONYL-COA
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 MUTATION: YES
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 1CML    1       VERSN
REVDAT   4   24-FEB-09 1CML    1       VERSN
REVDAT   3   01-APR-03 1CML    1       JRNL
REVDAT   2   05-OCT-99 1CML    1       HEADER KEYWDS JRNL
REVDAT   1   18-AUG-99 1CML    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.    1.69 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) : 1.69
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 84.52
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000
REMARK   3   COMPLETENESS FOR RANGE        (%) : 97.4
REMARK   3   NUMBER OF REFLECTIONS             : 39507
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) : 0.167
REMARK   3   FREE R VALUE                     : 0.200
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000
REMARK   3   FREE R VALUE TEST SET COUNT      : 1975
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 2994
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 77
REMARK   3   SOLVENT ATOMS            : 399
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) : 0.011 ; NULL
REMARK   3    ANGLE DISTANCE                  (A) : 2.141 ; 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 1CML COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 31-MAR-99.
REMARK 100 THE RCSB ID CODE IS RCSB000758.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : JUL-98
REMARK 200  TEMPERATURE           (KELVIN) : 105.00
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   : 39507
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.690
REMARK 200  RESOLUTION RANGE LOW       (A) : 84.520
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 97.3
REMARK 200  DATA REDUNDANCY                : 2.160
REMARK 200  R MERGE                    (I) : NULL
REMARK 200  R SYM                      (I) : 0.02600
REMARK 200   FOR THE DATA SET  : 15.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.69
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.73
REMARK 200  COMPLETENESS FOR SHELL     (%) : 83.2
REMARK 200  DATA REDUNDANCY IN SHELL       : 1.70
REMARK 200  R MERGE FOR SHELL          (I) : NULL
REMARK 200  R SYM FOR SHELL            (I) : 0.08900
REMARK 200   FOR SHELL         : 7.900
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: 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       43.48533
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       21.74267
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       21.74267
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       43.48533
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: 10630 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 26070 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -69.0 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      130.45600
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   O    HOH A   627     O    HOH A   683              2.17
REMARK 500   O    HOH A   719     O    HOH A   752              2.19
REMARK 500
REMARK 500 REMARK: NULL
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   O    HOH A   536     O    HOH A   760     4557     1.20
REMARK 500   O    HOH A   620     O    HOH A   620     4557     1.70
REMARK 500   O    HOH A   669     O    HOH A   767     4556     1.95
REMARK 500   O    HOH A   546     O    HOH A   616     6656     2.03
REMARK 500   O    HOH A   618     O    HOH A   619     4557     2.05
REMARK 500   O    HOH A   596     O    HOH A   780     6656     2.09
REMARK 500   O    HOH A   761     O    HOH A   563     2664     2.10
REMARK 500   O    HOH A   552     O    HOH A   566     5666     2.14
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   8   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.4 DEGREES
REMARK 500    ARG A  58   NE  -  CZ  -  NH1 ANGL. DEV. =   5.0 DEGREES
REMARK 500    ARG A  58   NE  -  CZ  -  NH2 ANGL. DEV. =  -6.1 DEGREES
REMARK 500    ARG A  67   CD  -  NE  -  CZ  ANGL. DEV. =  21.3 DEGREES
REMARK 500    ARG A  67   NE  -  CZ  -  NH1 ANGL. DEV. =   7.6 DEGREES
REMARK 500    ARG A  67   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.6 DEGREES
REMARK 500    MET A 137   CG  -  SD  -  CE  ANGL. DEV. = -11.6 DEGREES
REMARK 500    PRO A 138   N   -  CA  -  CB  ANGL. DEV. =   6.8 DEGREES
REMARK 500    ARG A 156   NE  -  CZ  -  NH1 ANGL. DEV. =   4.0 DEGREES
REMARK 500    ASP A 207   CB  -  CG  -  OD1 ANGL. DEV. =   7.5 DEGREES
REMARK 500    VAL A 342   CB  -  CA  -  C   ANGL. DEV. =  13.9 DEGREES
REMARK 500    VAL A 342   N   -  CA  -  CB  ANGL. DEV. = -18.5 DEGREES
REMARK 500    ARG A 350   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.1 DEGREES
REMARK 500    GLY A 376   CA  -  C   -  N   ANGL. DEV. =  16.8 DEGREES
REMARK 500    GLY A 376   O   -  C   -  N   ANGL. DEV. = -14.0 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    ALA A  21      142.47   -171.79
REMARK 500    SER A  90        3.17   -163.86
REMARK 500    GLU A 231       -5.06     67.06
REMARK 500    LYS A 269     -135.41   -136.26
REMARK 500    TYR A 334      -11.88   -141.30
REMARK 500    MET A 337       32.85    -99.02
REMARK 500    SER A 338     -136.35     51.59
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        -10.72
REMARK 500    ASN A  82        -11.73
REMARK 500    PHE A 265         15.80
REMARK 500    SER A 276        -10.61
REMARK 500    THR A 354        -16.14
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 604        DISTANCE =  5.21 ANGSTROMS
REMARK 525    HOH A 664        DISTANCE =  6.93 ANGSTROMS
REMARK 525    HOH A 728        DISTANCE =  6.24 ANGSTROMS
REMARK 600
REMARK 600 HETEROGEN
REMARK 600 APPEARS DECARBOXYLATED IN THE DENSITY
REMARK 615
REMARK 615 ZERO OCCUPANCY ATOM
REMARK 615 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 615 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 615 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 615 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 615   M RES C SSEQI
REMARK 615     MLC A  390
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: CYS
REMARK 800 EVIDENCE_CODE: AUTHOR
REMARK 800 SITE_DESCRIPTION: CATALYTIC SITE, INACTIVATED BY MUTATION C164A
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 392
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MLC A 390
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PIN A 391
DBREF  1CML A    1   389  UNP    P30074   CHS2_MEDSA       1    389
SEQADV 1CML ALA A  164  UNP  P30074    CYS   164 ENGINEERED
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 ALA 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    SO4  A 392       5
HET    MLC  A 390      54
HET    PIN  A 391      18
HETNAM     SO4 SULFATE ION
HETNAM     MLC MALONYL-COENZYME A
HETNAM     PIN PIPERAZINE-N,N'-BIS(2-ETHANESULFONIC ACID)
HETSYN     PIN PIPES; 1,4-PIPERAZINEDIETHANESULFONIC ACID
FORMUL   2  SO4    O4 S 2-
FORMUL   3  MLC    C24 H38 N7 O19 P3 S
FORMUL   4  PIN    C8 H18 N2 O6 S2
FORMUL   5  HOH   *399(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 ALA 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 ARG A 185  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 2 ILE A 254  ARG A 259  0
SHEET    2   C 2 GLY A 262  LEU A 267 -1  N  HIS A 266   O  ASP A 255
SHEET    1   D 4 PHE A 299  ALA A 302  0
SHEET    2   D 4 TRP A 367  GLY A 374  1  N  VAL A 369   O  PHE A 299
SHEET    3   D 4 THR A 378  SER A 386 -1  N  LEU A 384   O  GLY A 368
SHEET    4   D 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       -16.38
CISPEP   2 GLY A  376    LEU A  377          0         2.04
SITE     1 CYS  1 ALA A 164
SITE     1 AC1  6 VAL A   2  SER A   3  VAL A   4  SER A   5
SITE     2 AC1  6 ARG A 385  HOH A 606
SITE     1 AC2 17 LYS A  55  ARG A  58  MET A  59  LYS A  62
SITE     2 AC2 17 VAL A 210  PHE A 215  PHE A 265  LEU A 267
SITE     3 AC2 17 PRO A 272  GLY A 305  GLY A 306  PRO A 307
SITE     4 AC2 17 ALA A 308  PIN A 391  HOH A 457  HOH A 648
SITE     5 AC2 17 HOH A 717
SITE     1 AC3 11 ALA A 164  VAL A 210  LEU A 214  VAL A 271
SITE     2 AC3 11 PRO A 272  HIS A 303  GLY A 305  ASN A 336
SITE     3 AC3 11 PHE A 373  MLC A 390  HOH A 486
CRYST1   97.768   97.768   65.228  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      0.010228  0.005905  0.000000        0.00000
SCALE2      0.000000  0.011811  0.000000        0.00000
SCALE3      0.000000  0.000000  0.015331        0.00000
      
PROCHECK
Go to PROCHECK summary
 References