HEADER TRANSFERASE 22-FEB-08 3CBG
TITLE FUNCTIONAL AND STRUCTURAL CHARACTERIZATION OF A CATIONDEPENDENT O-
TITLE 2 METHYLTRANSFERASE FROM THE CYANOBACTERIUM SYNECHOCYSTIS SP. STRAIN
TITLE 3 PCC 6803
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: O-METHYLTRANSFERASE;
COMPND 3 CHAIN: A;
COMPND 4 EC: 2.1.1.-;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SYNECHOCYSTIS SP.;
SOURCE 3 ORGANISM_TAXID: 1148;
SOURCE 4 STRAIN: PCC 6803;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: M15 PREP4;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PQE30
KEYWDS O-METHYLTRANSFERASE, CYANOBACTERIUM, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR J.G.KOPYCKI,P.NEUMANN,M.T.STUBBS
REVDAT 5 01-NOV-23 3CBG 1 REMARK SEQADV LINK
REVDAT 4 25-OCT-17 3CBG 1 REMARK
REVDAT 3 24-FEB-09 3CBG 1 VERSN
REVDAT 2 05-AUG-08 3CBG 1 JRNL
REVDAT 1 10-JUN-08 3CBG 0
JRNL AUTH J.G.KOPYCKI,M.T.STUBBS,W.BRANDT,M.HAGEMANN,A.PORZEL,
JRNL AUTH 2 J.SCHMIDT,W.SCHLIEMANN,M.H.ZENK,T.VOGT
JRNL TITL FUNCTIONAL AND STRUCTURAL CHARACTERIZATION OF A
JRNL TITL 2 CATION-DEPENDENT O-METHYLTRANSFERASE FROM THE CYANOBACTERIUM
JRNL TITL 3 SYNECHOCYSTIS SP. STRAIN PCC 6803
JRNL REF J.BIOL.CHEM. V. 283 20888 2008
JRNL REFN ISSN 0021-9258
JRNL PMID 18502765
JRNL DOI 10.1074/JBC.M801943200
REMARK 2
REMARK 2 RESOLUTION. 2.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 28.81
REMARK 3 DATA CUTOFF (SIGMA(F)) : 1.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 16164
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 SET) : 0.152
REMARK 3 FREE R VALUE : 0.216
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 9.200
REMARK 3 FREE R VALUE TEST SET COUNT : 1485
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : NULL
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : NULL
REMARK 3 BIN RESOLUTION RANGE LOW (A) : NULL
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : NULL
REMARK 3 BIN FREE R VALUE : NULL
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : NULL
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1697
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 55
REMARK 3 SOLVENT ATOMS : 124
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 28.89
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -2.18700
REMARK 3 B22 (A**2) : -2.18700
REMARK 3 B33 (A**2) : 4.37300
REMARK 3 B12 (A**2) : -2.30200
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM SIGMAA (A) : NULL
REMARK 3 LOW RESOLUTION CUTOFF (A) : NULL
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM C-V SIGMAA (A) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.006
REMARK 3 BOND ANGLES (DEGREES) : 1.235
REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL
REMARK 3 IMPROPER ANGLES (DEGREES) : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : 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 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : NULL
REMARK 3 KSOL : NULL
REMARK 3 BSOL : 46.45
REMARK 3
REMARK 3 NCS MODEL : NULL
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : PROTEIN_REP.PARAM
REMARK 3 PARAMETER FILE 2 : SYN_LIG.PARAM
REMARK 3 PARAMETER FILE 3 : ION.PARAM
REMARK 3 PARAMETER FILE 4 : WATER_REP.PARAM
REMARK 3 PARAMETER FILE 5 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3 TOPOLOGY FILE 2 : NULL
REMARK 3 TOPOLOGY FILE 3 : NULL
REMARK 3 TOPOLOGY FILE 4 : NULL
REMARK 3 TOPOLOGY FILE 5 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HEMIHEDRALLY TWINNED; THIS IS A TWINNED
REMARK 3 DATA. THE TWINNING OPERATOR IS (H,K,L) -> (-H, -K, L) AND THE
REMARK 3 TWINNING FRACTION IS 0.284.
REMARK 4
REMARK 4 3CBG COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 26-FEB-08.
REMARK 100 THE DEPOSITION ID IS D_1000046574.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 06-FEB-07
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.5
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 MICROMAX-007
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 IV
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO, HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK, HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 16207
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 8.700
REMARK 200 R MERGE (I) : 0.12400
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 9.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.07
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.9
REMARK 200 DATA REDUNDANCY IN SHELL : 6.90
REMARK 200 R MERGE FOR SHELL (I) : 0.70300
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> 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: PHASER
REMARK 200 STARTING MODEL: PDB ENTRY 3C3Y
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 44.87
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.23
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 30% PEG 4000 (W/V), 0.2M MGCL2 IN 0.1M
REMARK 280 TRIS/HCL, PH 8.5, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31 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+1/3
REMARK 290 3555 -X+Y,-X,Z+2/3
REMARK 290 4555 Y,X,-Z
REMARK 290 5555 X-Y,-Y,-Z+2/3
REMARK 290 6555 -X,-X+Y,-Z+1/3
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 39.94467
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 79.88933
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 79.88933
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 39.94467
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
REMARK 350 TOTAL BURIED SURFACE AREA: 4260 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 17070 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -21.0 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 -86.43300
REMARK 350 BIOMT2 2 0.866025 0.500000 0.000000 49.90212
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH A1251 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 -11
REMARK 465 ARG A -10
REMARK 465 GLY A -9
REMARK 465 SER A -8
REMARK 465 HIS A -7
REMARK 465 HIS A -6
REMARK 465 HIS A -5
REMARK 465 HIS A -4
REMARK 465 HIS A -3
REMARK 465 HIS A -2
REMARK 465 GLY A -1
REMARK 465 SER A 0
REMARK 465 MET A 1
REMARK 465 GLY A 2
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 LYS A 132 CG CD CE NZ
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 PHE A 70 -130.12 64.01
REMARK 500 ASP A 143 51.16 -156.98
REMARK 500 ALA A 144 -146.01 -121.69
REMARK 500 ASN A 170 33.08 73.88
REMARK 500 TRP A 173 73.25 18.63
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A 401 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 143 OD1
REMARK 620 2 ASP A 169 OD2 86.8
REMARK 620 3 ASN A 170 OD1 83.8 85.7
REMARK 620 4 FER A 501 O4 81.8 161.7 78.8
REMARK 620 5 4FE A 502 O3 158.8 113.9 93.1 77.0
REMARK 620 6 4FE A 502 O4 84.5 160.6 76.1 3.9 74.5
REMARK 620 7 HOH A1128 O 92.8 91.2 175.5 103.6 91.2 106.5
REMARK 620 N 1 2 3 4 5 6
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SAH A 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FER A 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 4FE A 502
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3C3Y RELATED DB: PDB
REMARK 900 O-METHYLTRANSFERASE FROM M. CRYSTALLINUM
DBREF 3CBG A 1 220 UNP Q55813 Q55813_SYNY3 1 220
SEQADV 3CBG MET A -11 UNP Q55813 INITIATING METHIONINE
SEQADV 3CBG ARG A -10 UNP Q55813 EXPRESSION TAG
SEQADV 3CBG GLY A -9 UNP Q55813 EXPRESSION TAG
SEQADV 3CBG SER A -8 UNP Q55813 EXPRESSION TAG
SEQADV 3CBG HIS A -7 UNP Q55813 EXPRESSION TAG
SEQADV 3CBG HIS A -6 UNP Q55813 EXPRESSION TAG
SEQADV 3CBG HIS A -5 UNP Q55813 EXPRESSION TAG
SEQADV 3CBG HIS A -4 UNP Q55813 EXPRESSION TAG
SEQADV 3CBG HIS A -3 UNP Q55813 EXPRESSION TAG
SEQADV 3CBG HIS A -2 UNP Q55813 EXPRESSION TAG
SEQADV 3CBG GLY A -1 UNP Q55813 EXPRESSION TAG
SEQADV 3CBG SER A 0 UNP Q55813 EXPRESSION TAG
SEQRES 1 A 232 MET ARG GLY SER HIS HIS HIS HIS HIS HIS GLY SER MET
SEQRES 2 A 232 GLY LYS GLY ILE THR GLY PHE ASP PRO SER LEU TYR SER
SEQRES 3 A 232 TYR LEU GLN SER ILE SER ALA ASP ASP SER PHE TYR LEU
SEQRES 4 A 232 ALA GLN LEU ARG ARG GLU THR ALA HIS LEU PRO GLY ALA
SEQRES 5 A 232 PRO MET GLN ILE SER PRO GLU GLN ALA GLN PHE LEU GLY
SEQRES 6 A 232 LEU LEU ILE SER LEU THR GLY ALA LYS GLN VAL LEU GLU
SEQRES 7 A 232 ILE GLY VAL PHE ARG GLY TYR SER ALA LEU ALA MET ALA
SEQRES 8 A 232 LEU GLN LEU PRO PRO ASP GLY GLN ILE ILE ALA CYS ASP
SEQRES 9 A 232 GLN ASP PRO ASN ALA THR ALA ILE ALA LYS LYS TYR TRP
SEQRES 10 A 232 GLN LYS ALA GLY VAL ALA GLU LYS ILE SER LEU ARG LEU
SEQRES 11 A 232 GLY PRO ALA LEU ALA THR LEU GLU GLN LEU THR GLN GLY
SEQRES 12 A 232 LYS PRO LEU PRO GLU PHE ASP LEU ILE PHE ILE ASP ALA
SEQRES 13 A 232 ASP LYS ARG ASN TYR PRO ARG TYR TYR GLU ILE GLY LEU
SEQRES 14 A 232 ASN LEU LEU ARG ARG GLY GLY LEU MET VAL ILE ASP ASN
SEQRES 15 A 232 VAL LEU TRP HIS GLY LYS VAL THR GLU VAL ASP PRO GLN
SEQRES 16 A 232 GLU ALA GLN THR GLN VAL LEU GLN GLN PHE ASN ARG ASP
SEQRES 17 A 232 LEU ALA GLN ASP GLU ARG VAL ARG ILE SER VAL ILE PRO
SEQRES 18 A 232 LEU GLY ASP GLY MET THR LEU ALA LEU LYS LYS
HET MG A 401 1
HET SAH A 301 26
HET FER A 501 14
HET 4FE A 502 14
HETNAM MG MAGNESIUM ION
HETNAM SAH S-ADENOSYL-L-HOMOCYSTEINE
HETNAM FER 3-(4-HYDROXY-3-METHOXYPHENYL)-2-PROPENOIC ACID
HETNAM 4FE (2E)-3-(3-HYDROXY-4-METHOXYPHENYL)PROP-2-ENOIC ACID
HETSYN FER FERULIC ACID
HETSYN 4FE 3-(3-HYDROXY-4-METHOXYPHENYL)-2-PROPENOIC ACID
FORMUL 2 MG MG 2+
FORMUL 3 SAH C14 H20 N6 O5 S
FORMUL 4 FER C10 H10 O4
FORMUL 5 4FE C10 H10 O4
FORMUL 6 HOH *124(H2 O)
HELIX 1 1 ASP A 9 ILE A 19 1 11
HELIX 2 2 SER A 24 THR A 34 1 11
HELIX 3 3 GLY A 39 GLN A 43 5 5
HELIX 4 4 SER A 45 GLY A 60 1 16
HELIX 5 5 GLY A 72 LEU A 80 1 9
HELIX 6 6 ASP A 94 ALA A 108 1 15
HELIX 7 7 VAL A 110 GLU A 112 5 3
HELIX 8 8 PRO A 120 GLN A 130 1 11
HELIX 9 9 ASP A 145 ARG A 147 5 3
HELIX 10 10 ASN A 148 LEU A 159 1 12
HELIX 11 11 LEU A 172 GLU A 179 5 8
HELIX 12 12 GLU A 184 ALA A 198 1 15
SHEET 1 A 7 ILE A 114 LEU A 118 0
SHEET 2 A 7 GLN A 87 ASP A 92 1 N ALA A 90 O ARG A 117
SHEET 3 A 7 GLN A 63 ILE A 67 1 N VAL A 64 O GLN A 87
SHEET 4 A 7 PHE A 137 ILE A 142 1 O ASP A 138 N GLN A 63
SHEET 5 A 7 LEU A 160 ASP A 169 1 O VAL A 167 N ILE A 140
SHEET 6 A 7 MET A 214 LYS A 219 -1 O ALA A 217 N MET A 166
SHEET 7 A 7 VAL A 203 ILE A 208 -1 N ILE A 208 O MET A 214
LINK OD1 ASP A 143 MG MG A 401 1555 1555 2.36
LINK OD2 ASP A 169 MG MG A 401 1555 1555 2.41
LINK OD1 ASN A 170 MG MG A 401 1555 1555 2.24
LINK MG MG A 401 O4 AFER A 501 1555 1555 2.43
LINK MG MG A 401 O3 B4FE A 502 1555 1555 2.20
LINK MG MG A 401 O4 B4FE A 502 1555 1555 2.28
LINK MG MG A 401 O HOH A1128 1555 1555 2.43
CISPEP 1 LYS A 132 PRO A 133 0 -0.12
SITE 1 AC1 5 MET A 42 ASP A 143 ASP A 169 ASN A 170
SITE 2 AC1 5 HOH A1128
SITE 1 AC2 18 GLN A 43 ILE A 44 GLY A 68 PHE A 70
SITE 2 AC2 18 TYR A 73 SER A 74 ASP A 92 GLN A 93
SITE 3 AC2 18 PRO A 120 ALA A 121 ASP A 143 ALA A 144
SITE 4 AC2 18 ASP A 145 TYR A 152 HOH A1141 HOH A1142
SITE 5 AC2 18 HOH A1258 HOH A1259
SITE 1 AC3 5 MET A 42 ASP A 143 LYS A 146 ASN A 170
SITE 2 AC3 5 HIS A 174
SITE 1 AC4 6 LYS A 3 MET A 42 ASP A 143 LYS A 146
SITE 2 AC4 6 ASN A 170 HIS A 174
CRYST1 57.622 57.622 119.834 90.00 90.00 120.00 P 31 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 0.017354 0.010020 0.000000 0.00000
SCALE2 0.000000 0.020039 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008345 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
