HEADER TRANSFERASE 28-MAR-09 3GU3
TITLE CRYSTAL STRUCTURE OF THE METHYLTRANSFERASE BC_2162 IN COMPLEX WITH S-
TITLE 2 ADENOSYL-L-HOMOCYSTEINE FROM BACILLUS CEREUS, NORTHEAST STRUCTURAL
TITLE 3 GENOMICS CONSORTIUM TARGET BCR20
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: METHYLTRANSFERASE;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: BC_2162;
COMPND 5 EC: 2.1.1.-;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BACILLUS CEREUS;
SOURCE 3 ORGANISM_TAXID: 226900;
SOURCE 4 STRAIN: ATCC 14579;
SOURCE 5 GENE: BC_2162;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)+ MAGIC;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET21
KEYWDS ALPHA-BETA PROTEIN, STRUCTURAL GENOMICS, PSI-2, PROTEIN STRUCTURE
KEYWDS 2 INITIATIVE, NORTHEAST STRUCTURAL GENOMICS CONSORTIUM, NESG,
KEYWDS 3 METHYLTRANSFERASE, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR F.FOROUHAR,H.NEELY,J.SEETHARAMAN,C.CIANO,L.MA,L.ZHAO,J.K.EVERETT,
AUTHOR 2 R.NAIR,T.B.ACTON,B.ROST,G.T.MONTELIONE,L.TONG,J.F.HUNT,NORTHEAST
AUTHOR 3 STRUCTURAL GENOMICS CONSORTIUM (NESG)
REVDAT 5 24-JUL-19 3GU3 1 REMARK LINK
REVDAT 4 01-NOV-17 3GU3 1 REMARK
REVDAT 3 24-AUG-11 3GU3 1 AUTHOR
REVDAT 2 13-JUL-11 3GU3 1 VERSN
REVDAT 1 07-APR-09 3GU3 0
JRNL AUTH F.FOROUHAR,H.NEELY,J.SEETHARAMAN,C.CIANO,L.MA,L.ZHAO,
JRNL AUTH 2 J.K.EVERETT,R.NAIR,T.B.ACTON,B.ROST,G.T.MONTELIONE,L.TONG,
JRNL AUTH 3 J.F.HUNT
JRNL TITL NORTHEAST STRUCTURAL GENOMICS CONSORTIUM TARGET BCR20
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.30 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.2 & XTALVIEW
REMARK 3 AUTHORS : NULL
REMARK 3
REMARK 3 REFINEMENT TARGET : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.30
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.92
REMARK 3 DATA CUTOFF (SIGMA(F)) : 2.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 314365.531
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 88.8
REMARK 3 NUMBER OF REFLECTIONS : 89210
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) : 0.184
REMARK 3 FREE R VALUE : 0.212
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.900
REMARK 3 FREE R VALUE TEST SET COUNT : 4337
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.003
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 10
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.30
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.38
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 71.10
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 6875
REMARK 3 BIN R VALUE (WORKING SET) : 0.2170
REMARK 3 BIN FREE R VALUE : 0.2410
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 4.40
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 319
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.013
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4424
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 60
REMARK 3 SOLVENT ATOMS : 293
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 20.10
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 35.20
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.41000
REMARK 3 B22 (A**2) : 0.41000
REMARK 3 B33 (A**2) : -0.83000
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 COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.23
REMARK 3 ESD FROM SIGMAA (A) : 0.22
REMARK 3 LOW RESOLUTION CUTOFF (A) : 5.00
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.27
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.23
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.007
REMARK 3 BOND ANGLES (DEGREES) : 1.200
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 23.00
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.740
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : RESTRAINED
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 : FLAT MODEL
REMARK 3 KSOL : 0.45
REMARK 3 BSOL : 58.80
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 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 3GU3 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 31-MAR-09.
REMARK 100 THE DEPOSITION ID IS D_1000052307.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 10-AUG-07
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 4
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : NSLS
REMARK 200 BEAMLINE : X4A
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97905
REMARK 200 MONOCHROMATOR : SI 111 CHANNEL
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 4
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 100246
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.300
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 200 DATA REDUNDANCY : 3.800
REMARK 200 R MERGE (I) : 0.08300
REMARK 200 R SYM (I) : 0.06600
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 14.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.30
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.38
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 3.80
REMARK 200 R MERGE FOR SHELL (I) : 0.49000
REMARK 200 R SYM FOR SHELL (I) : 0.47900
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.980
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD
REMARK 200 SOFTWARE USED: SNB & SOLVE/RESOLVE
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 72.23
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.43
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PROTEIN SOLUTION: 100MM NACL, 5MM DTT,
REMARK 280 0.02% NAN3, 10MM TRIS-HCL (PH 7.5), AND 10MM S-ADENOSYL-L-
REMARK 280 METHIONINE . RESERVOIR SOLUTION: 100 MM SODIUM CITRATE AND 5.76M
REMARK 280 POTASSIUM ACETATE , VAPOR DIFFUSION, HANGING DROP, TEMPERATURE
REMARK 280 277K, PH 4
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32
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
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 81.75133
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 40.87567
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: 4200 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 23620 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -21.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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 LEU A 294
REMARK 465 GLU A 295
REMARK 465 HIS A 296
REMARK 465 HIS A 297
REMARK 465 HIS A 298
REMARK 465 HIS A 299
REMARK 465 HIS A 300
REMARK 465 HIS A 301
REMARK 465 LEU B 294
REMARK 465 GLU B 295
REMARK 465 HIS B 296
REMARK 465 HIS B 297
REMARK 465 HIS B 298
REMARK 465 HIS B 299
REMARK 465 HIS B 300
REMARK 465 HIS B 301
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 PRO A 88 30.80 -86.06
REMARK 500 SER A 152 53.31 -93.48
REMARK 500 ARG A 179 -95.93 -80.55
REMARK 500 PRO B 88 30.77 -86.12
REMARK 500 SER B 152 53.30 -93.55
REMARK 500 ARG B 179 -95.87 -80.32
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 ACT A 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SAH A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT B 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SAH B 401
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2GH1 RELATED DB: PDB
REMARK 900 2GH1 IS THE CRYSTAL STRUCTURE OF THE APO ENZYME.
REMARK 900 RELATED ID: BCR20 RELATED DB: TARGETDB
DBREF 3GU3 A 18 293 UNP Q81E32 Q81E32_BACCR 18 293
DBREF 3GU3 B 18 293 UNP Q81E32 Q81E32_BACCR 18 293
SEQADV 3GU3 LEU A 294 UNP Q81E32 EXPRESSION TAG
SEQADV 3GU3 GLU A 295 UNP Q81E32 EXPRESSION TAG
SEQADV 3GU3 HIS A 296 UNP Q81E32 EXPRESSION TAG
SEQADV 3GU3 HIS A 297 UNP Q81E32 EXPRESSION TAG
SEQADV 3GU3 HIS A 298 UNP Q81E32 EXPRESSION TAG
SEQADV 3GU3 HIS A 299 UNP Q81E32 EXPRESSION TAG
SEQADV 3GU3 HIS A 300 UNP Q81E32 EXPRESSION TAG
SEQADV 3GU3 HIS A 301 UNP Q81E32 EXPRESSION TAG
SEQADV 3GU3 LEU B 294 UNP Q81E32 EXPRESSION TAG
SEQADV 3GU3 GLU B 295 UNP Q81E32 EXPRESSION TAG
SEQADV 3GU3 HIS B 296 UNP Q81E32 EXPRESSION TAG
SEQADV 3GU3 HIS B 297 UNP Q81E32 EXPRESSION TAG
SEQADV 3GU3 HIS B 298 UNP Q81E32 EXPRESSION TAG
SEQADV 3GU3 HIS B 299 UNP Q81E32 EXPRESSION TAG
SEQADV 3GU3 HIS B 300 UNP Q81E32 EXPRESSION TAG
SEQADV 3GU3 HIS B 301 UNP Q81E32 EXPRESSION TAG
SEQRES 1 A 284 ARG ASP LEU TYR TYR ASN ASP ASP TYR VAL SER PHE LEU
SEQRES 2 A 284 VAL ASN THR VAL TRP LYS ILE THR LYS PRO VAL HIS ILE
SEQRES 3 A 284 VAL ASP TYR GLY CYS GLY TYR GLY TYR LEU GLY LEU VAL
SEQRES 4 A 284 LEU MSE PRO LEU LEU PRO GLU GLY SER LYS TYR THR GLY
SEQRES 5 A 284 ILE ASP SER GLY GLU THR LEU LEU ALA GLU ALA ARG GLU
SEQRES 6 A 284 LEU PHE ARG LEU LEU PRO TYR ASP SER GLU PHE LEU GLU
SEQRES 7 A 284 GLY ASP ALA THR GLU ILE GLU LEU ASN ASP LYS TYR ASP
SEQRES 8 A 284 ILE ALA ILE CYS HIS ALA PHE LEU LEU HIS MSE THR THR
SEQRES 9 A 284 PRO GLU THR MSE LEU GLN LYS MSE ILE HIS SER VAL LYS
SEQRES 10 A 284 LYS GLY GLY LYS ILE ILE CYS PHE GLU PRO HIS TRP ILE
SEQRES 11 A 284 SER ASN MSE ALA SER TYR LEU LEU ASP GLY GLU LYS GLN
SEQRES 12 A 284 SER GLU PHE ILE GLN LEU GLY VAL LEU GLN LYS LEU PHE
SEQRES 13 A 284 GLU SER ASP THR GLN ARG ASN GLY LYS ASP GLY ASN ILE
SEQRES 14 A 284 GLY MSE LYS ILE PRO ILE TYR LEU SER GLU LEU GLY VAL
SEQRES 15 A 284 LYS ASN ILE GLU CYS ARG VAL SER ASP LYS VAL ASN PHE
SEQRES 16 A 284 LEU ASP SER ASN MSE HIS HIS ASN ASP LYS ASN ASP LEU
SEQRES 17 A 284 TYR GLN SER LEU LYS GLU GLU GLY ILE ALA GLY ASP PRO
SEQRES 18 A 284 GLY ASP LYS GLN GLN PHE VAL GLU ARG LEU ILE ALA ARG
SEQRES 19 A 284 GLY LEU THR TYR ASP ASN ALA LEU ALA GLN TYR GLU ALA
SEQRES 20 A 284 GLU LEU ARG PHE PHE LYS ALA LEU HIS LEU HIS SER SER
SEQRES 21 A 284 LEU VAL TYR ALA PRO ASN MSE LYS ILE THR PHE GLY GLU
SEQRES 22 A 284 ILE GLU CYS LEU GLU HIS HIS HIS HIS HIS HIS
SEQRES 1 B 284 ARG ASP LEU TYR TYR ASN ASP ASP TYR VAL SER PHE LEU
SEQRES 2 B 284 VAL ASN THR VAL TRP LYS ILE THR LYS PRO VAL HIS ILE
SEQRES 3 B 284 VAL ASP TYR GLY CYS GLY TYR GLY TYR LEU GLY LEU VAL
SEQRES 4 B 284 LEU MSE PRO LEU LEU PRO GLU GLY SER LYS TYR THR GLY
SEQRES 5 B 284 ILE ASP SER GLY GLU THR LEU LEU ALA GLU ALA ARG GLU
SEQRES 6 B 284 LEU PHE ARG LEU LEU PRO TYR ASP SER GLU PHE LEU GLU
SEQRES 7 B 284 GLY ASP ALA THR GLU ILE GLU LEU ASN ASP LYS TYR ASP
SEQRES 8 B 284 ILE ALA ILE CYS HIS ALA PHE LEU LEU HIS MSE THR THR
SEQRES 9 B 284 PRO GLU THR MSE LEU GLN LYS MSE ILE HIS SER VAL LYS
SEQRES 10 B 284 LYS GLY GLY LYS ILE ILE CYS PHE GLU PRO HIS TRP ILE
SEQRES 11 B 284 SER ASN MSE ALA SER TYR LEU LEU ASP GLY GLU LYS GLN
SEQRES 12 B 284 SER GLU PHE ILE GLN LEU GLY VAL LEU GLN LYS LEU PHE
SEQRES 13 B 284 GLU SER ASP THR GLN ARG ASN GLY LYS ASP GLY ASN ILE
SEQRES 14 B 284 GLY MSE LYS ILE PRO ILE TYR LEU SER GLU LEU GLY VAL
SEQRES 15 B 284 LYS ASN ILE GLU CYS ARG VAL SER ASP LYS VAL ASN PHE
SEQRES 16 B 284 LEU ASP SER ASN MSE HIS HIS ASN ASP LYS ASN ASP LEU
SEQRES 17 B 284 TYR GLN SER LEU LYS GLU GLU GLY ILE ALA GLY ASP PRO
SEQRES 18 B 284 GLY ASP LYS GLN GLN PHE VAL GLU ARG LEU ILE ALA ARG
SEQRES 19 B 284 GLY LEU THR TYR ASP ASN ALA LEU ALA GLN TYR GLU ALA
SEQRES 20 B 284 GLU LEU ARG PHE PHE LYS ALA LEU HIS LEU HIS SER SER
SEQRES 21 B 284 LEU VAL TYR ALA PRO ASN MSE LYS ILE THR PHE GLY GLU
SEQRES 22 B 284 ILE GLU CYS LEU GLU HIS HIS HIS HIS HIS HIS
MODRES 3GU3 MSE A 58 MET SELENOMETHIONINE
MODRES 3GU3 MSE A 119 MET SELENOMETHIONINE
MODRES 3GU3 MSE A 125 MET SELENOMETHIONINE
MODRES 3GU3 MSE A 129 MET SELENOMETHIONINE
MODRES 3GU3 MSE A 150 MET SELENOMETHIONINE
MODRES 3GU3 MSE A 188 MET SELENOMETHIONINE
MODRES 3GU3 MSE A 217 MET SELENOMETHIONINE
MODRES 3GU3 MSE A 284 MET SELENOMETHIONINE
MODRES 3GU3 MSE B 58 MET SELENOMETHIONINE
MODRES 3GU3 MSE B 119 MET SELENOMETHIONINE
MODRES 3GU3 MSE B 125 MET SELENOMETHIONINE
MODRES 3GU3 MSE B 129 MET SELENOMETHIONINE
MODRES 3GU3 MSE B 150 MET SELENOMETHIONINE
MODRES 3GU3 MSE B 188 MET SELENOMETHIONINE
MODRES 3GU3 MSE B 217 MET SELENOMETHIONINE
MODRES 3GU3 MSE B 284 MET SELENOMETHIONINE
HET MSE A 58 8
HET MSE A 119 8
HET MSE A 125 8
HET MSE A 129 8
HET MSE A 150 8
HET MSE A 188 8
HET MSE A 217 8
HET MSE A 284 8
HET MSE B 58 8
HET MSE B 119 8
HET MSE B 125 8
HET MSE B 129 8
HET MSE B 150 8
HET MSE B 188 8
HET MSE B 217 8
HET MSE B 284 8
HET ACT A 302 4
HET SAH A 401 26
HET ACT B 302 4
HET SAH B 401 26
HETNAM MSE SELENOMETHIONINE
HETNAM ACT ACETATE ION
HETNAM SAH S-ADENOSYL-L-HOMOCYSTEINE
FORMUL 1 MSE 16(C5 H11 N O2 SE)
FORMUL 3 ACT 2(C2 H3 O2 1-)
FORMUL 4 SAH 2(C14 H20 N6 O5 S)
FORMUL 7 HOH *293(H2 O)
HELIX 1 1 ASN A 23 THR A 33 1 11
HELIX 2 2 GLY A 51 MSE A 58 1 8
HELIX 3 3 GLY A 73 LEU A 86 1 14
HELIX 4 4 PHE A 115 MSE A 119 5 5
HELIX 5 5 THR A 121 SER A 132 1 12
HELIX 6 6 HIS A 145 SER A 152 1 8
HELIX 7 7 LYS A 159 ILE A 164 1 6
HELIX 8 8 GLN A 165 ASN A 180 1 16
HELIX 9 9 ASN A 185 MSE A 188 5 4
HELIX 10 10 LYS A 189 LEU A 197 1 9
HELIX 11 11 HIS A 219 GLU A 232 1 14
HELIX 12 12 ASP A 240 ALA A 250 1 11
HELIX 13 13 THR A 254 LEU A 272 1 19
HELIX 14 14 ASN B 23 THR B 33 1 11
HELIX 15 15 GLY B 51 MSE B 58 1 8
HELIX 16 16 GLY B 73 LEU B 86 1 14
HELIX 17 17 PHE B 115 MSE B 119 5 5
HELIX 18 18 THR B 121 SER B 132 1 12
HELIX 19 19 HIS B 145 SER B 152 1 8
HELIX 20 20 LYS B 159 ILE B 164 1 6
HELIX 21 21 GLN B 165 ASN B 180 1 16
HELIX 22 22 ASN B 185 MSE B 188 5 4
HELIX 23 23 LYS B 189 LEU B 197 1 9
HELIX 24 24 HIS B 219 GLU B 232 1 14
HELIX 25 25 ASP B 240 ALA B 250 1 11
HELIX 26 26 THR B 254 LEU B 272 1 19
SHEET 1 A 7 ASP A 90 GLU A 95 0
SHEET 2 A 7 LYS A 66 ASP A 71 1 N GLY A 69 O LEU A 94
SHEET 3 A 7 HIS A 42 TYR A 46 1 N ASP A 45 O THR A 68
SHEET 4 A 7 TYR A 107 HIS A 113 1 O ILE A 111 N VAL A 44
SHEET 5 A 7 VAL A 133 GLU A 143 1 O LYS A 138 N ASP A 108
SHEET 6 A 7 LYS A 285 GLU A 290 -1 O THR A 287 N CYS A 141
SHEET 7 A 7 LYS A 200 VAL A 206 -1 N LYS A 200 O GLU A 290
SHEET 1 B 3 TYR A 153 LEU A 155 0
SHEET 2 B 3 LEU A 278 TYR A 280 -1 O VAL A 279 N LEU A 154
SHEET 3 B 3 ASN A 211 LEU A 213 -1 N ASN A 211 O TYR A 280
SHEET 1 C 7 ASP B 90 GLU B 95 0
SHEET 2 C 7 LYS B 66 ASP B 71 1 N GLY B 69 O LEU B 94
SHEET 3 C 7 HIS B 42 TYR B 46 1 N ASP B 45 O THR B 68
SHEET 4 C 7 TYR B 107 HIS B 113 1 O ILE B 111 N VAL B 44
SHEET 5 C 7 VAL B 133 GLU B 143 1 O LYS B 138 N ASP B 108
SHEET 6 C 7 LYS B 285 GLU B 290 -1 O THR B 287 N CYS B 141
SHEET 7 C 7 LYS B 200 VAL B 206 -1 N LYS B 200 O GLU B 290
SHEET 1 D 3 TYR B 153 LEU B 155 0
SHEET 2 D 3 LEU B 278 TYR B 280 -1 O VAL B 279 N LEU B 154
SHEET 3 D 3 ASN B 211 LEU B 213 -1 N ASN B 211 O TYR B 280
LINK C LEU A 57 N MSE A 58 1555 1555 1.33
LINK C MSE A 58 N PRO A 59 1555 1555 1.34
LINK C HIS A 118 N MSE A 119 1555 1555 1.33
LINK C MSE A 119 N THR A 120 1555 1555 1.33
LINK C THR A 124 N MSE A 125 1555 1555 1.33
LINK C MSE A 125 N LEU A 126 1555 1555 1.33
LINK C LYS A 128 N MSE A 129 1555 1555 1.33
LINK C MSE A 129 N ILE A 130 1555 1555 1.33
LINK C ASN A 149 N MSE A 150 1555 1555 1.34
LINK C MSE A 150 N ALA A 151 1555 1555 1.33
LINK C GLY A 187 N MSE A 188 1555 1555 1.33
LINK C MSE A 188 N LYS A 189 1555 1555 1.33
LINK C ASN A 216 N MSE A 217 1555 1555 1.33
LINK C MSE A 217 N HIS A 218 1555 1555 1.32
LINK C ASN A 283 N MSE A 284 1555 1555 1.32
LINK C MSE A 284 N LYS A 285 1555 1555 1.33
LINK C LEU B 57 N MSE B 58 1555 1555 1.33
LINK C MSE B 58 N PRO B 59 1555 1555 1.34
LINK C HIS B 118 N MSE B 119 1555 1555 1.33
LINK C MSE B 119 N THR B 120 1555 1555 1.33
LINK C THR B 124 N MSE B 125 1555 1555 1.33
LINK C MSE B 125 N LEU B 126 1555 1555 1.33
LINK C LYS B 128 N MSE B 129 1555 1555 1.33
LINK C MSE B 129 N ILE B 130 1555 1555 1.33
LINK C ASN B 149 N MSE B 150 1555 1555 1.33
LINK C MSE B 150 N ALA B 151 1555 1555 1.33
LINK C GLY B 187 N MSE B 188 1555 1555 1.32
LINK C MSE B 188 N LYS B 189 1555 1555 1.33
LINK C ASN B 216 N MSE B 217 1555 1555 1.32
LINK C MSE B 217 N HIS B 218 1555 1555 1.33
LINK C ASN B 283 N MSE B 284 1555 1555 1.32
LINK C MSE B 284 N LYS B 285 1555 1555 1.33
SITE 1 AC1 3 ASN A 104 ASP A 105 TYR A 107
SITE 1 AC2 17 GLY A 47 CYS A 48 GLY A 49 TYR A 52
SITE 2 AC2 17 ASP A 71 SER A 72 GLY A 96 ASP A 97
SITE 3 AC2 17 ALA A 98 HIS A 113 ALA A 114 PHE A 115
SITE 4 AC2 17 MSE A 119 HOH A 384 HOH A 386 HOH A 395
SITE 5 AC2 17 HOH A 404
SITE 1 AC3 4 LEU B 103 ASN B 104 ASP B 105 TYR B 107
SITE 1 AC4 15 GLY B 47 CYS B 48 GLY B 49 TYR B 52
SITE 2 AC4 15 ASP B 71 SER B 72 GLY B 96 ASP B 97
SITE 3 AC4 15 ALA B 98 HIS B 113 ALA B 114 PHE B 115
SITE 4 AC4 15 MSE B 119 HOH B 315 HOH B 380
CRYST1 90.793 90.793 122.627 90.00 90.00 120.00 P 32 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 0.011014 0.006359 0.000000 0.00000
SCALE2 0.000000 0.012718 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008155 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
