HEADER TRANSFERASE 13-SEP-97 1JMH
TITLE CONTRIBUTIONS OF ORIENTATION AND HYDROGEN BONDING TO CATALYSIS IN ASN-
TITLE 2 229 MUTANTS OF THYMIDYLATE SYNTHASE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: THYMIDYLATE SYNTHASE;
COMPND 3 CHAIN: A;
COMPND 4 EC: 2.1.1.45;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: LACTOBACILLUS CASEI;
SOURCE 3 ORGANISM_TAXID: 1582;
SOURCE 4 GENE: N229I MUTANT OF CLONED L. CASE;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: CHI-2913, LACKING A THYMIDYLATE SYNTHASE
SOURCE 8 GENE;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PSCTS9;
SOURCE 10 EXPRESSION_SYSTEM_GENE: N229I MUTANT OF CLONED L. CASEI TS
KEYWDS TRANSFERASE, METHYLTRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR J.FINER-MOORE,R.M.STROUD
REVDAT 6 07-FEB-24 1JMH 1 REMARK
REVDAT 5 03-NOV-21 1JMH 1 REMARK SEQADV
REVDAT 4 16-NOV-11 1JMH 1 HETATM
REVDAT 3 13-JUL-11 1JMH 1 VERSN
REVDAT 2 24-FEB-09 1JMH 1 VERSN
REVDAT 1 28-JAN-98 1JMH 0
JRNL AUTH J.S.FINER-MOORE,L.LIU,D.L.BIRDSALL,R.BREM,J.APFELD,
JRNL AUTH 2 D.V.SANTI,R.M.STROUD
JRNL TITL CONTRIBUTIONS OF ORIENTATION AND HYDROGEN BONDING TO
JRNL TITL 2 CATALYSIS IN ASN229 MUTANTS OF THYMIDYLATE SYNTHASE.
JRNL REF J.MOL.BIOL. V. 276 113 1998
JRNL REFN ISSN 0022-2836
JRNL PMID 9514716
JRNL DOI 10.1006/JMBI.1997.1495
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH J.S.FINER-MOORE,L.LIU,C.E.SCHAFMEISTER,D.L.BIRDSALL,T.MAU,
REMARK 1 AUTH 2 D.V.SANTI,R.M.STROUD
REMARK 1 TITL PARTITIONING ROLES OF SIDE CHAINS IN AFFINITY, ORIENTATION,
REMARK 1 TITL 2 AND CATALYSIS WITH STRUCTURES FOR MUTANT COMPLEXES:
REMARK 1 TITL 3 ASPARAGINE-229 IN THYMIDYLATE SYNTHASE
REMARK 1 REF BIOCHEMISTRY V. 35 5125 1996
REMARK 1 REFN ISSN 0006-2960
REMARK 1 REFERENCE 2
REMARK 1 AUTH R.M.STROUD,J.S.FINER-MOORE
REMARK 1 TITL STEREOCHEMISTRY OF A MULTISTEP/BIPARTITE METHYL TRANSFER
REMARK 1 TITL 2 REACTION: THYMIDYLATE SYNTHASE
REMARK 1 REF FASEB J. V. 7 671 1993
REMARK 1 REFN ISSN 0892-6638
REMARK 1 REFERENCE 3
REMARK 1 AUTH J.FINER-MOORE,E.B.FAUMAN,P.G.FOSTER,K.M.PERRY,D.V.SANTI,
REMARK 1 AUTH 2 R.M.STROUD
REMARK 1 TITL REFINED STRUCTURES OF SUBSTRATE-BOUND AND PHOSPHATE-BOUND
REMARK 1 TITL 2 THYMIDYLATE SYNTHASE FROM LACTOBACILLUS CASEI
REMARK 1 REF J.MOL.BIOL. V. 232 1101 1993
REMARK 1 REFN ISSN 0022-2836
REMARK 1 REFERENCE 4
REMARK 1 AUTH L.LIU,D.V.SANTI
REMARK 1 TITL ASPARAGINE 229 IN THYMIDYLATE SYNTHASE CONTRIBUTES TO, BUT
REMARK 1 TITL 2 IS NOT ESSENTIAL FOR, CATALYSIS
REMARK 1 REF PROC.NATL.ACAD.SCI.USA V. 90 8604 1993
REMARK 1 REFN ISSN 0027-8424
REMARK 2
REMARK 2 RESOLUTION. 2.50 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 7.00
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) (%) : 82.0
REMARK 3 NUMBER OF REFLECTIONS : 12491
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : NULL
REMARK 3 R VALUE (WORKING SET) : 0.213
REMARK 3 FREE R VALUE : 0.311
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : NULL
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 : 2593
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 20
REMARK 3 SOLVENT ATOMS : 80
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 27.00
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 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) : 0.008
REMARK 3 BOND ANGLES (DEGREES) : 1.600
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 24.60
REMARK 3 IMPROPER ANGLES (DEGREES) : 1.300
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 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 : PARAM11.DNA
REMARK 3 PARAMETER FILE 2 : NULL
REMARK 3 PARAMETER FILE 3 : NULL
REMARK 3 TOPOLOGY FILE 1 : TOPH11.DNA
REMARK 3 TOPOLOGY FILE 2 : NULL
REMARK 3 TOPOLOGY FILE 3 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1JMH COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 100 THE DEPOSITION ID IS D_1000174348.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 23-OCT-94
REMARK 200 TEMPERATURE (KELVIN) : NULL
REMARK 200 PH : 7.4
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : NULL
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : NULL
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
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : R-AXIS II
REMARK 200 DATA SCALING SOFTWARE : NULL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 15136
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.500
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 93.0
REMARK 200 DATA REDUNDANCY : 3.000
REMARK 200 R MERGE (I) : 0.14100
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: NULL
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL
REMARK 200 SOFTWARE USED: X-PLOR
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 55.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.94
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PH 7.4
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 61 2 2
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 -X,-Y,Z+1/2
REMARK 290 5555 Y,-X+Y,Z+5/6
REMARK 290 6555 X-Y,X,Z+1/6
REMARK 290 7555 Y,X,-Z+1/3
REMARK 290 8555 X-Y,-Y,-Z
REMARK 290 9555 -X,-X+Y,-Z+2/3
REMARK 290 10555 -Y,-X,-Z+5/6
REMARK 290 11555 -X+Y,Y,-Z+1/2
REMARK 290 12555 X,X-Y,-Z+1/6
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 80.83333
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 161.66667
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 121.25000
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 202.08333
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 40.41667
REMARK 290 SMTRY1 7 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 7 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 80.83333
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 9 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 9 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 9 0.000000 0.000000 -1.000000 161.66667
REMARK 290 SMTRY1 10 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 10 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 10 0.000000 0.000000 -1.000000 202.08333
REMARK 290 SMTRY1 11 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 11 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 11 0.000000 0.000000 -1.000000 121.25000
REMARK 290 SMTRY1 12 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 12 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 12 0.000000 0.000000 -1.000000 40.41667
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: 5840 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 25940 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -24.0 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 -1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 -121.25000
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 464 LIES ON A SPECIAL POSITION.
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 460 O HOH A 460 11554 0.85
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 THR A 24 -93.95 -62.51
REMARK 500 HIS A 25 -29.97 -166.12
REMARK 500 PRO A 45 38.95 -69.69
REMARK 500 LYS A 50 130.48 -175.66
REMARK 500 PRO A 53 94.24 -62.56
REMARK 500 THR A 69 10.26 -145.13
REMARK 500 MET A 101 13.12 54.21
REMARK 500 PHE A 104 -179.18 -61.47
REMARK 500 LYS A 110 -81.15 -129.17
REMARK 500 ALA A 152 55.15 -152.55
REMARK 500 TYR A 176 30.14 -88.06
REMARK 500 VAL A 190 -38.44 -32.88
REMARK 500 PRO A 276 152.53 -43.42
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: CAT
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: CATALYTIC CYSTEINE.
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE UMP A 317
DBREF 1JMH A 1 316 UNP P00469 TYSY_LACCA 1 316
SEQADV 1JMH ILE A 229 UNP P00469 ASN 229 ENGINEERED MUTATION
SEQRES 1 A 316 MET LEU GLU GLN PRO TYR LEU ASP LEU ALA LYS LYS VAL
SEQRES 2 A 316 LEU ASP GLU GLY HIS PHE LYS PRO ASP ARG THR HIS THR
SEQRES 3 A 316 GLY THR TYR SER ILE PHE GLY HIS GLN MET ARG PHE ASP
SEQRES 4 A 316 LEU SER LYS GLY PHE PRO LEU LEU THR THR LYS LYS VAL
SEQRES 5 A 316 PRO PHE GLY LEU ILE LYS SER GLU LEU LEU TRP PHE LEU
SEQRES 6 A 316 HIS GLY ASP THR ASN ILE ARG PHE LEU LEU GLN HIS ARG
SEQRES 7 A 316 ASN HIS ILE TRP ASP GLU TRP ALA PHE GLU LYS TRP VAL
SEQRES 8 A 316 LYS SER ASP GLU TYR HIS GLY PRO ASP MET THR ASP PHE
SEQRES 9 A 316 GLY HIS ARG SER GLN LYS ASP PRO GLU PHE ALA ALA VAL
SEQRES 10 A 316 TYR HIS GLU GLU MET ALA LYS PHE ASP ASP ARG VAL LEU
SEQRES 11 A 316 HIS ASP ASP ALA PHE ALA ALA LYS TYR GLY ASP LEU GLY
SEQRES 12 A 316 LEU VAL TYR GLY SER GLN TRP ARG ALA TRP HIS THR SER
SEQRES 13 A 316 LYS GLY ASP THR ILE ASP GLN LEU GLY ASP VAL ILE GLU
SEQRES 14 A 316 GLN ILE LYS THR HIS PRO TYR SER ARG ARG LEU ILE VAL
SEQRES 15 A 316 SER ALA TRP ASN PRO GLU ASP VAL PRO THR MET ALA LEU
SEQRES 16 A 316 PRO PRO CYS HIS THR LEU TYR GLN PHE TYR VAL ASN ASP
SEQRES 17 A 316 GLY LYS LEU SER LEU GLN LEU TYR GLN ARG SER ALA ASP
SEQRES 18 A 316 ILE PHE LEU GLY VAL PRO PHE ILE ILE ALA SER TYR ALA
SEQRES 19 A 316 LEU LEU THR HIS LEU VAL ALA HIS GLU CYS GLY LEU GLU
SEQRES 20 A 316 VAL GLY GLU PHE ILE HIS THR PHE GLY ASP ALA HIS LEU
SEQRES 21 A 316 TYR VAL ASN HIS LEU ASP GLN ILE LYS GLU GLN LEU SER
SEQRES 22 A 316 ARG THR PRO ARG PRO ALA PRO THR LEU GLN LEU ASN PRO
SEQRES 23 A 316 ASP LYS HIS ASP ILE PHE ASP PHE ASP MET LYS ASP ILE
SEQRES 24 A 316 LYS LEU LEU ASN TYR ASP PRO TYR PRO ALA ILE LYS ALA
SEQRES 25 A 316 PRO VAL ALA VAL
HET UMP A 317 20
HETNAM UMP 2'-DEOXYURIDINE 5'-MONOPHOSPHATE
HETSYN UMP DUMP
FORMUL 2 UMP C9 H13 N2 O8 P
FORMUL 3 HOH *80(H2 O)
HELIX 1 1 GLN A 4 GLU A 16 1 13
HELIX 2 2 PHE A 54 LEU A 65 1 12
HELIX 3 3 ILE A 71 HIS A 77 1 7
HELIX 4 4 ASP A 83 VAL A 91 1 9
HELIX 5 5 ARG A 107 GLN A 109 5 3
HELIX 6 6 PRO A 112 HIS A 131 1 20
HELIX 7 7 ASP A 133 TYR A 139 1 7
HELIX 8 8 TYR A 146 ARG A 151 1 6
HELIX 9 9 GLN A 163 THR A 173 1 11
HELIX 10 10 PRO A 187 VAL A 190 1 4
HELIX 11 11 VAL A 226 GLU A 243 1 18
HELIX 12 12 VAL A 262 SER A 273 5 12
HELIX 13 13 MET A 296 ASP A 298 5 3
SHEET 1 A 4 HIS A 18 PRO A 21 0
SHEET 2 A 4 GLY A 27 PHE A 32 -1 N SER A 30 O HIS A 18
SHEET 3 A 4 ASP A 257 TYR A 261 -1 N LEU A 260 O TYR A 29
SHEET 4 A 4 SER A 219 ASP A 221 1 N ALA A 220 O ASP A 257
SHEET 1 B 5 HIS A 34 ASP A 39 0
SHEET 2 B 5 GLU A 250 PHE A 255 -1 N PHE A 255 O HIS A 34
SHEET 3 B 5 LYS A 210 GLN A 217 1 N LEU A 213 O ILE A 252
SHEET 4 B 5 HIS A 199 ASN A 207 -1 N ASN A 207 O LYS A 210
SHEET 5 B 5 ILE A 181 SER A 183 -1 N VAL A 182 O TYR A 202
SHEET 1 C 2 THR A 281 LEU A 284 0
SHEET 2 C 2 ILE A 299 LEU A 302 -1 N LEU A 302 O THR A 281
SITE 1 CAT 1 CYS A 198
SITE 1 AC1 11 ARG A 178 ARG A 179 LEU A 195 GLN A 217
SITE 2 AC1 11 ARG A 218 SER A 219 ALA A 220 ASP A 221
SITE 3 AC1 11 GLY A 225 HIS A 259 TYR A 261
CRYST1 78.400 78.400 242.500 90.00 90.00 120.00 P 61 2 2 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 0.012755 0.007364 0.000000 0.00000
SCALE2 0.000000 0.014728 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004124 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
