HEADER TRANSFERASE 23-SEP-00 1FWM
TITLE CRYSTAL STRUCTURE OF THE THYMIDYLATE SYNTHASE R166Q MUTANT
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: THYMIDYLATE SYNTHASE;
COMPND 3 CHAIN: A, B;
COMPND 4 EC: 2.1.1.45;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 562;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS METHYLTRANSFERASE, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR R.R.SOTELO-MUNDO,L.CHANGCHIEN,F.MALEY,W.R.MONTFORT
REVDAT 8 03-NOV-21 1FWM 1 REMARK SEQADV LINK
REVDAT 7 18-APR-18 1FWM 1 REMARK
REVDAT 6 04-OCT-17 1FWM 1 REMARK
REVDAT 5 13-JUL-11 1FWM 1 VERSN
REVDAT 4 03-NOV-09 1FWM 1 HETATM
REVDAT 3 24-FEB-09 1FWM 1 VERSN
REVDAT 2 25-APR-06 1FWM 1 JRNL
REVDAT 1 11-NOV-03 1FWM 0
JRNL AUTH R.R.SOTELO-MUNDO,L.CHANGCHIEN,F.MALEY,W.R.MONTFORT
JRNL TITL CRYSTAL STRUCTURES OF THYMIDYLATE SYNTHASE MUTANT R166Q:
JRNL TITL 2 STRUCTURAL BASIS FOR THE NEARLY COMPLETE LOSS OF CATALYTIC
JRNL TITL 3 ACTIVITY.
JRNL REF J.BIOCHEM.MOL.TOXICOL. V. 20 88 2006
JRNL REFN ISSN 1095-6670
JRNL PMID 16615077
JRNL DOI 10.1002/JBT.20122
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH R.R.SOTELO-MUNDO
REMARK 1 TITL CRYSTALLOGRAPHICS STUDIED OF THYMIDYLATE SYNTHASE: STRUCTURE
REMARK 1 TITL 2 OF A MAMMALIAN ENZYME AND ANALYSES OF INVARIANT
REMARK 1 TITL 3 NON-CATALYTIC RESIDUES IN A BACTERIAL ENZYME
REMARK 1 REF THESIS 1 1999
REMARK 2
REMARK 2 RESOLUTION. 2.20 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) : 2.20
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 17.95
REMARK 3 DATA CUTOFF (SIGMA(F)) : 3.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 2512983.040
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 79.6
REMARK 3 NUMBER OF REFLECTIONS : 25280
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) : 0.180
REMARK 3 FREE R VALUE : 0.225
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 9.900
REMARK 3 FREE R VALUE TEST SET COUNT : 2493
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.004
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 6
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.20
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.34
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 57.00
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 2708
REMARK 3 BIN R VALUE (WORKING SET) : 0.2120
REMARK 3 BIN FREE R VALUE : 0.2510
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 9.80
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 295
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.015
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4302
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 80
REMARK 3 SOLVENT ATOMS : 170
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 10.70
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 28.00
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -1.45000
REMARK 3 B22 (A**2) : -1.45000
REMARK 3 B33 (A**2) : 2.91000
REMARK 3 B12 (A**2) : -0.25000
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) : 0.22
REMARK 3 ESD FROM SIGMAA (A) : 0.21
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) : 0.29
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.26
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.011
REMARK 3 BOND ANGLES (DEGREES) : 1.700
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 25.40
REMARK 3 IMPROPER ANGLES (DEGREES) : 1.480
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 : 0.33
REMARK 3 BSOL : 42.73
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 : CBX.PAR
REMARK 3 PARAMETER FILE 3 : WATER_REP.PARAM
REMARK 3 PARAMETER FILE 4 : CB3.PAR
REMARK 3 PARAMETER FILE 5 : ION.PARAM
REMARK 3 PARAMETER FILE 6 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : CBX.TOP
REMARK 3 TOPOLOGY FILE 3 : WATER.TOP
REMARK 3 TOPOLOGY FILE 4 : CB3.TOP
REMARK 3 TOPOLOGY FILE 5 : ION.TOP
REMARK 3 TOPOLOGY FILE 6 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1FWM COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 03-OCT-00.
REMARK 100 THE DEPOSITION ID IS D_1000011960.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 13-OCT-97
REMARK 200 TEMPERATURE (KELVIN) : 298
REMARK 200 PH : 8.0
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 : ENRAF-NONIUS FR571
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 : DIFFRACTOMETER
REMARK 200 DETECTOR MANUFACTURER : ENRAF-NONIUS FAST
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : ROTAVATA, MADNESS
REMARK 200 DATA SCALING SOFTWARE : CCP4 (AGROVATA, ROTAVATA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 31445
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.200
REMARK 200 RESOLUTION RANGE LOW (A) : 18.137
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.2
REMARK 200 DATA REDUNDANCY : 3.100
REMARK 200 R MERGE (I) : 0.09000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 6.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.20
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.26
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.5
REMARK 200 DATA REDUNDANCY IN SHELL : 2.50
REMARK 200 R MERGE FOR SHELL (I) : 0.38000
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: NULL
REMARK 200 SOFTWARE USED: CNS
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 52.35
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.58
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: AMMONIUM SULFATE, POTASSIUM SULFATE,
REMARK 280 EDTA, DTT, PH 8.0, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE
REMARK 280 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 63
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z
REMARK 290 3555 -X+Y,-X,Z
REMARK 290 4555 -X,-Y,Z+1/2
REMARK 290 5555 Y,-X+Y,Z+1/2
REMARK 290 6555 X-Y,X,Z+1/2
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 0.00000
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 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 33.83500
REMARK 290 SMTRY1 5 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 5 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 33.83500
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 33.83500
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 300 REMARK: THE BIOLOGICAL ASSEMBLY IS A DIMER CONSTRUCTED FROM CHAINS
REMARK 300 A AND B. BOTH DIMERS ARE CONTAINED IN THE ASSYMETRIC UNIT IN THIS
REMARK 300 SPACE GROUP
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: 7170 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 19710 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -65.0 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 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 LYS A 48 145.51 -173.71
REMARK 500 PRO A 92 71.32 -69.51
REMARK 500 TYR A 94 -64.87 -26.36
REMARK 500 ALA A 100 64.37 -154.53
REMARK 500 ASP A 122 52.72 -141.64
REMARK 500 ILE B 369 4.61 -66.84
REMARK 500 TYR B 394 -72.08 -19.70
REMARK 500 ALA B 400 69.84 -152.54
REMARK 500 LEU B 443 143.26 -174.55
REMARK 500 ASP B 505 99.30 -69.25
REMARK 500 PRO B 528 -165.87 -69.27
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 SO4 A 265
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 565
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CB3 A 266
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CB3 B 566
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1FFL RELATED DB: PDB
REMARK 900 1FFL CONTAINS THE SAME PROTEIN IN THE ABSENCE OF LIGANDS (APO-TS)
DBREF 1FWM A 1 264 UNP P0A884 TYSY_ECOLI 1 264
DBREF 1FWM B 301 564 UNP P0A884 TYSY_ECOLI 1 264
SEQADV 1FWM CXM A 1 UNP P0A884 MET 1 MODIFIED RESIDUE
SEQADV 1FWM GLN A 166 UNP P0A884 ARG 166 ENGINEERED MUTATION
SEQADV 1FWM CXM B 301 UNP P0A884 MET 1 MODIFIED RESIDUE
SEQADV 1FWM GLN B 466 UNP P0A884 ARG 166 ENGINEERED MUTATION
SEQRES 1 A 264 CXM LYS GLN TYR LEU GLU LEU MET GLN LYS VAL LEU ASP
SEQRES 2 A 264 GLU GLY THR GLN LYS ASN ASP ARG THR GLY THR GLY THR
SEQRES 3 A 264 LEU SER ILE PHE GLY HIS GLN MET ARG PHE ASN LEU GLN
SEQRES 4 A 264 ASP GLY PHE PRO LEU VAL THR THR LYS ARG CYS HIS LEU
SEQRES 5 A 264 ARG SER ILE ILE HIS GLU LEU LEU TRP PHE LEU GLN GLY
SEQRES 6 A 264 ASP THR ASN ILE ALA TYR LEU HIS GLU ASN ASN VAL THR
SEQRES 7 A 264 ILE TRP ASP GLU TRP ALA ASP GLU ASN GLY ASP LEU GLY
SEQRES 8 A 264 PRO VAL TYR GLY LYS GLN TRP ARG ALA TRP PRO THR PRO
SEQRES 9 A 264 ASP GLY ARG HIS ILE ASP GLN ILE THR THR VAL LEU ASN
SEQRES 10 A 264 GLN LEU LYS ASN ASP PRO ASP SER ARG ARG ILE ILE VAL
SEQRES 11 A 264 SER ALA TRP ASN VAL GLY GLU LEU ASP LYS MET ALA LEU
SEQRES 12 A 264 ALA PRO CYS HIS ALA PHE PHE GLN PHE TYR VAL ALA ASP
SEQRES 13 A 264 GLY LYS LEU SER CYS GLN LEU TYR GLN GLN SER CYS ASP
SEQRES 14 A 264 VAL PHE LEU GLY LEU PRO PHE ASN ILE ALA SER TYR ALA
SEQRES 15 A 264 LEU LEU VAL HIS MET MET ALA GLN GLN CYS ASP LEU GLU
SEQRES 16 A 264 VAL GLY ASP PHE VAL TRP THR GLY GLY ASP THR HIS LEU
SEQRES 17 A 264 TYR SER ASN HIS MET ASP GLN THR HIS LEU GLN LEU SER
SEQRES 18 A 264 ARG GLU PRO ARG PRO LEU PRO LYS LEU ILE ILE LYS ARG
SEQRES 19 A 264 LYS PRO GLU SER ILE PHE ASP TYR ARG PHE GLU ASP PHE
SEQRES 20 A 264 GLU ILE GLU GLY TYR ASP PRO HIS PRO GLY ILE LYS ALA
SEQRES 21 A 264 PRO VAL ALA ILE
SEQRES 1 B 264 CXM LYS GLN TYR LEU GLU LEU MET GLN LYS VAL LEU ASP
SEQRES 2 B 264 GLU GLY THR GLN LYS ASN ASP ARG THR GLY THR GLY THR
SEQRES 3 B 264 LEU SER ILE PHE GLY HIS GLN MET ARG PHE ASN LEU GLN
SEQRES 4 B 264 ASP GLY PHE PRO LEU VAL THR THR LYS ARG CYS HIS LEU
SEQRES 5 B 264 ARG SER ILE ILE HIS GLU LEU LEU TRP PHE LEU GLN GLY
SEQRES 6 B 264 ASP THR ASN ILE ALA TYR LEU HIS GLU ASN ASN VAL THR
SEQRES 7 B 264 ILE TRP ASP GLU TRP ALA ASP GLU ASN GLY ASP LEU GLY
SEQRES 8 B 264 PRO VAL TYR GLY LYS GLN TRP ARG ALA TRP PRO THR PRO
SEQRES 9 B 264 ASP GLY ARG HIS ILE ASP GLN ILE THR THR VAL LEU ASN
SEQRES 10 B 264 GLN LEU LYS ASN ASP PRO ASP SER ARG ARG ILE ILE VAL
SEQRES 11 B 264 SER ALA TRP ASN VAL GLY GLU LEU ASP LYS MET ALA LEU
SEQRES 12 B 264 ALA PRO CYS HIS ALA PHE PHE GLN PHE TYR VAL ALA ASP
SEQRES 13 B 264 GLY LYS LEU SER CYS GLN LEU TYR GLN GLN SER CYS ASP
SEQRES 14 B 264 VAL PHE LEU GLY LEU PRO PHE ASN ILE ALA SER TYR ALA
SEQRES 15 B 264 LEU LEU VAL HIS MET MET ALA GLN GLN CYS ASP LEU GLU
SEQRES 16 B 264 VAL GLY ASP PHE VAL TRP THR GLY GLY ASP THR HIS LEU
SEQRES 17 B 264 TYR SER ASN HIS MET ASP GLN THR HIS LEU GLN LEU SER
SEQRES 18 B 264 ARG GLU PRO ARG PRO LEU PRO LYS LEU ILE ILE LYS ARG
SEQRES 19 B 264 LYS PRO GLU SER ILE PHE ASP TYR ARG PHE GLU ASP PHE
SEQRES 20 B 264 GLU ILE GLU GLY TYR ASP PRO HIS PRO GLY ILE LYS ALA
SEQRES 21 B 264 PRO VAL ALA ILE
MODRES 1FWM CXM A 1 MET N-CARBOXYMETHIONINE
MODRES 1FWM CXM B 301 MET N-CARBOXYMETHIONINE
HET CXM A 1 11
HET CXM B 301 11
HET SO4 A 265 5
HET SO4 A 565 5
HET CB3 A 266 35
HET CB3 B 566 35
HETNAM CXM N-CARBOXYMETHIONINE
HETNAM SO4 SULFATE ION
HETNAM CB3 10-PROPARGYL-5,8-DIDEAZAFOLIC ACID
FORMUL 1 CXM 2(C6 H11 N O4 S)
FORMUL 3 SO4 2(O4 S 2-)
FORMUL 5 CB3 2(C24 H23 N5 O6)
FORMUL 7 HOH *170(H2 O)
HELIX 1 1 LYS A 2 GLY A 15 1 14
HELIX 2 2 HIS A 51 GLN A 64 1 14
HELIX 3 3 ILE A 69 ASN A 75 1 7
HELIX 4 4 TRP A 80 ALA A 84 5 5
HELIX 5 5 VAL A 93 ALA A 100 1 8
HELIX 6 6 ASP A 110 ASP A 122 1 13
HELIX 7 7 ASN A 134 MET A 141 5 8
HELIX 8 8 LEU A 172 CYS A 192 1 21
HELIX 9 9 HIS A 212 SER A 221 1 10
HELIX 10 10 ARG A 243 GLU A 245 5 3
HELIX 11 11 LYS B 302 GLY B 315 1 14
HELIX 12 12 GLN B 339 GLY B 341 5 3
HELIX 13 13 HIS B 351 GLN B 364 1 14
HELIX 14 14 ILE B 369 ASN B 375 1 7
HELIX 15 15 TRP B 380 ALA B 384 5 5
HELIX 16 16 VAL B 393 ALA B 400 1 8
HELIX 17 17 ASP B 410 ASP B 422 1 13
HELIX 18 18 ASN B 434 MET B 441 5 8
HELIX 19 19 LEU B 472 CYS B 492 1 21
HELIX 20 20 HIS B 512 SER B 521 1 10
HELIX 21 21 ARG B 543 GLU B 545 5 3
SHEET 1 A 6 THR A 16 LYS A 18 0
SHEET 2 A 6 THR A 26 ASN A 37 -1 N THR A 26 O LYS A 18
SHEET 3 A 6 GLU A 195 TYR A 209 -1 N PHE A 199 O PHE A 36
SHEET 4 A 6 LYS A 158 ASP A 169 1 N LEU A 159 O GLU A 195
SHEET 5 A 6 PHE A 149 ALA A 155 -1 O PHE A 149 N TYR A 164
SHEET 6 A 6 ILE A 129 SER A 131 -1 N VAL A 130 O PHE A 150
SHEET 1 B 2 TRP A 101 PRO A 102 0
SHEET 2 B 2 HIS A 108 ILE A 109 -1 N ILE A 109 O TRP A 101
SHEET 1 C 2 LYS A 229 ILE A 232 0
SHEET 2 C 2 PHE A 247 GLU A 250 -1 O GLU A 248 N ILE A 231
SHEET 1 D 6 THR B 316 LYS B 318 0
SHEET 2 D 6 THR B 326 ASN B 337 -1 O THR B 326 N LYS B 318
SHEET 3 D 6 GLU B 495 TYR B 509 -1 N PHE B 499 O PHE B 336
SHEET 4 D 6 LYS B 458 ASP B 469 1 O LEU B 459 N GLY B 497
SHEET 5 D 6 PHE B 449 ALA B 455 -1 O PHE B 449 N TYR B 464
SHEET 6 D 6 ILE B 429 SER B 431 -1 N VAL B 430 O PHE B 450
SHEET 1 E 2 TRP B 401 PRO B 402 0
SHEET 2 E 2 HIS B 408 ILE B 409 -1 O ILE B 409 N TRP B 401
SHEET 1 F 2 LYS B 529 ILE B 532 0
SHEET 2 F 2 PHE B 547 GLU B 550 -1 O GLU B 548 N ILE B 531
LINK C CXM A 1 N LYS A 2 1555 1555 1.33
LINK C CXM B 301 N LYS B 302 1555 1555 1.33
SITE 1 AC1 6 ARG A 21 SER A 167 CB3 A 266 HOH A 641
SITE 2 AC1 6 ARG B 426 ARG B 427
SITE 1 AC2 6 ARG A 126 ARG A 127 HOH A 616 ARG B 321
SITE 2 AC2 6 SER B 467 CB3 B 566
SITE 1 AC3 17 GLU A 58 ILE A 79 TRP A 80 TRP A 83
SITE 2 AC3 17 TYR A 94 LEU A 143 ALA A 144 CYS A 146
SITE 3 AC3 17 PHE A 176 ASN A 177 LYS A 259 VAL A 262
SITE 4 AC3 17 SO4 A 265 HOH A 635 HOH A 639 HOH A 692
SITE 5 AC3 17 HOH A 732
SITE 1 AC4 15 SO4 A 565 HIS B 351 ILE B 379 TRP B 380
SITE 2 AC4 15 TRP B 383 TYR B 394 LEU B 443 ALA B 444
SITE 3 AC4 15 CYS B 446 GLY B 473 PHE B 476 ASN B 477
SITE 4 AC4 15 HOH B 620 HOH B 640 HOH B 753
CRYST1 127.060 127.060 67.670 90.00 90.00 120.00 P 63 12
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 0.007870 0.004544 0.000000 0.00000
SCALE2 0.000000 0.009088 0.000000 0.00000
SCALE3 0.000000 0.000000 0.014778 0.00000
HETATM 1 N CXM A 1 22.181 20.289 49.433 1.00 20.11 N
HETATM 2 CA CXM A 1 23.510 20.761 49.787 1.00 19.19 C
HETATM 3 CB CXM A 1 24.502 20.421 48.677 1.00 21.38 C
HETATM 4 CG CXM A 1 24.665 18.950 48.338 1.00 23.43 C
HETATM 5 SD CXM A 1 25.862 18.722 47.003 1.00 24.08 S
HETATM 6 CE CXM A 1 24.826 18.846 45.552 1.00 21.95 C
HETATM 7 C CXM A 1 23.497 22.271 49.969 1.00 20.70 C
HETATM 8 O CXM A 1 22.739 22.981 49.299 1.00 19.55 O
HETATM 9 CN CXM A 1 21.688 19.166 49.918 1.00 20.95 C
HETATM 10 ON1 CXM A 1 20.557 18.865 49.650 1.00 24.15 O
HETATM 11 ON2 CXM A 1 22.430 18.486 50.598 1.00 21.63 O
(ATOM LINES ARE NOT SHOWN.)
END
