HEADER ISOMERASE 01-NOV-99 1QO2
TITLE CRYSTAL STRUCTURE OF N-((5'-PHOSPHORIBOSYL)-FORMIMINO)-5-
TITLE 2 AMINOIMIDAZOL-4-CARBOXAMID RIBONUCLEOTID ISOMERASE (EC 3.1.3.15,
TITLE 3 HISA)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE:;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: HISA, PHOSPHORIBOSYLFORMIMINO-5-AMINOIMIDAZOLE CARBOXAMIDE
COMPND 5 RIBOTIDE ISOMERASE;
COMPND 6 EC: 5.3.1.15;
COMPND 7 ENGINEERED: YES;
COMPND 8 OTHER_DETAILS: M1, M17 AND M236 ARE SELENOMETHIONINE SUBSTITUTED
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: THERMOTOGA MARITIMA;
SOURCE 3 ORGANISM_TAXID: 2336;
SOURCE 4 CELLULAR_LOCATION: CYTOPLASM;
SOURCE 5 GENE: THISA;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: W3110 TRPEA2;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PDMI, 1
KEYWDS ISOMERASE, HISTIDINE BIOSYNTHESIS, THERMOPHILIC PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR M.WILMANNS,D.LANG,R.THOMA,R.STERNER
REVDAT 5 24-JUL-19 1QO2 1 REMARK
REVDAT 4 22-MAY-19 1QO2 1 REMARK LINK
REVDAT 3 24-FEB-09 1QO2 1 VERSN
REVDAT 2 02-SEP-00 1QO2 1 JRNL
REVDAT 1 12-JUL-00 1QO2 0
JRNL AUTH D.LANG,R.THOMA,M.HENN-SAX,R.STERNER,M.WILMANNS
JRNL TITL STRUCTURAL EVIDENCE FOR EVOLUTION OF THE BETA/ALPHA-BARREL
JRNL TITL 2 SCAFFOLD BY REPEATED GENE DUPLICATION AND FUSION
JRNL REF SCIENCE V. 289 1546 2000
JRNL REFN ISSN 0036-8075
JRNL PMID 10968789
JRNL DOI 10.1126/SCIENCE.289.5484.1546
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH R.THOMA,G.OBMOLOVA,D.A.LANG,M.SCHWANDER,P.JENOE,R.STERNER,
REMARK 1 AUTH 2 M.WILMANNS
REMARK 1 TITL EFFICIENT EXPRESSION, PURIFICATION AND CRYSTALLISATION OF
REMARK 1 TITL 2 TWO HYPERTHERMOSTABLE ENZYMES OF HISTIDINE BIOSYNTHESIS
REMARK 1 REF FEBS LETT. V. 454 1 1999
REMARK 1 REFN ISSN 0014-5793
REMARK 1 PMID 10413084
REMARK 1 DOI 10.1016/S0014-5793(99)00757-7
REMARK 2
REMARK 2 RESOLUTION. 1.85 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 0.9
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 : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.85
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 8.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 10000.000
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 97.4
REMARK 3 NUMBER OF REFLECTIONS : 34472
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) : 0.188
REMARK 3 FREE R VALUE : 0.246
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1707
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 : 34
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.85
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.87
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 78.64
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 855
REMARK 3 BIN R VALUE (WORKING SET) : 0.3060
REMARK 3 BIN FREE R VALUE : 0.3650
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5.00
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 58
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 : 3798
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 547
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 27.24
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 20.81
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -2.87800
REMARK 3 B22 (A**2) : 5.03700
REMARK 3 B33 (A**2) : -2.15900
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -3.64600
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.21
REMARK 3 ESD FROM SIGMAA (A) : 0.17
REMARK 3 LOW RESOLUTION CUTOFF (A) : 8.00
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.28
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.21
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.005
REMARK 3 BOND ANGLES (DEGREES) : 1.280
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 23.31
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.649
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) : 0.788 ; 9.000
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 1.293 ; 12.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 1.282 ; 12.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 1.987 ; 15.000
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : CNS DEFAULT, ANISOTROPIC B FACTORS
REMARK 3 KSOL : NULL
REMARK 3 BSOL : 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 : PROTEIN_REP.PARAM
REMARK 3 PARAMETER FILE 2 : WATER_REP.PARAM
REMARK 3 PARAMETER FILE 3 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : NULL
REMARK 3 TOPOLOGY FILE 3 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1QO2 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 01-NOV-99.
REMARK 100 THE DEPOSITION ID IS D_1290004335.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-JUN-98
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 5.60
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : EMBL/DESY, HAMBURG
REMARK 200 BEAMLINE : BW7A
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97893, 0.97929, 0.98089
REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL SI(111)
REMARK 200 OPTICS : RHODIUM COATED PRE-MIRROR
REMARK 200 FOCUSSING MIRROR
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 34932
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.850
REMARK 200 RESOLUTION RANGE LOW (A) : 39.841
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.4
REMARK 200 DATA REDUNDANCY : 3.510
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.04100
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 17.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.85
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.88
REMARK 200 COMPLETENESS FOR SHELL (%) : 91.9
REMARK 200 DATA REDUNDANCY IN SHELL : 1.95
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.26900
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.530
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: MAD
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD
REMARK 200 SOFTWARE USED: CNS 0.9, SHARP, SOLVE
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 31.86
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.82
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: SEE THOMA ET AL. (1999) FEBS LETTERS
REMARK 280 454, 1-6., PH 5.60
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y+1/2,-Z
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 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 36.58000
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PQS
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
REMARK 350 BIOMOLECULE: 2
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PQS
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 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 ARG A 241 CG CD NE CZ NH1 NH2
REMARK 470 ARG B 241 CG CD NE CZ NH1 NH2
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 ASN A 24 65.98 -119.74
REMARK 500 SER A 102 -82.42 -151.47
REMARK 500 SER B 102 -80.71 -154.43
REMARK 500 TRP B 138 19.07 173.58
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 A2040 DISTANCE = 5.82 ANGSTROMS
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1THF RELATED DB: PDB
DBREF 1QO2 A 1 241 UNP Q9X0C7 Q9X0C7 1 241
DBREF 1QO2 B 1 241 UNP Q9X0C7 Q9X0C7 1 241
SEQRES 1 A 241 MSE LEU VAL VAL PRO ALA ILE ASP LEU PHE ARG GLY LYS
SEQRES 2 A 241 VAL ALA ARG MSE ILE LYS GLY ARG LYS GLU ASN THR ILE
SEQRES 3 A 241 PHE TYR GLU LYS ASP PRO VAL GLU LEU VAL GLU LYS LEU
SEQRES 4 A 241 ILE GLU GLU GLY PHE THR LEU ILE HIS VAL VAL ASP LEU
SEQRES 5 A 241 SER ASN ALA ILE GLU ASN SER GLY GLU ASN LEU PRO VAL
SEQRES 6 A 241 LEU GLU LYS LEU SER GLU PHE ALA GLU HIS ILE GLN ILE
SEQRES 7 A 241 GLY GLY GLY ILE ARG SER LEU ASP TYR ALA GLU LYS LEU
SEQRES 8 A 241 ARG LYS LEU GLY TYR ARG ARG GLN ILE VAL SER SER LYS
SEQRES 9 A 241 VAL LEU GLU ASP PRO SER PHE LEU LYS SER LEU ARG GLU
SEQRES 10 A 241 ILE ASP VAL GLU PRO VAL PHE SER LEU ASP THR ARG GLY
SEQRES 11 A 241 GLY ARG VAL ALA PHE LYS GLY TRP LEU ALA GLU GLU GLU
SEQRES 12 A 241 ILE ASP PRO VAL SER LEU LEU LYS ARG LEU LYS GLU TYR
SEQRES 13 A 241 GLY LEU GLU GLU ILE VAL HIS THR GLU ILE GLU LYS ASP
SEQRES 14 A 241 GLY THR LEU GLN GLU HIS ASP PHE SER LEU THR LYS LYS
SEQRES 15 A 241 ILE ALA ILE GLU ALA GLU VAL LYS VAL LEU ALA ALA GLY
SEQRES 16 A 241 GLY ILE SER SER GLU ASN SER LEU LYS THR ALA GLN LYS
SEQRES 17 A 241 VAL HIS THR GLU THR ASN GLY LEU LEU LYS GLY VAL ILE
SEQRES 18 A 241 VAL GLY ARG ALA PHE LEU GLU GLY ILE LEU THR VAL GLU
SEQRES 19 A 241 VAL MSE LYS ARG TYR ALA ARG
SEQRES 1 B 241 MSE LEU VAL VAL PRO ALA ILE ASP LEU PHE ARG GLY LYS
SEQRES 2 B 241 VAL ALA ARG MSE ILE LYS GLY ARG LYS GLU ASN THR ILE
SEQRES 3 B 241 PHE TYR GLU LYS ASP PRO VAL GLU LEU VAL GLU LYS LEU
SEQRES 4 B 241 ILE GLU GLU GLY PHE THR LEU ILE HIS VAL VAL ASP LEU
SEQRES 5 B 241 SER ASN ALA ILE GLU ASN SER GLY GLU ASN LEU PRO VAL
SEQRES 6 B 241 LEU GLU LYS LEU SER GLU PHE ALA GLU HIS ILE GLN ILE
SEQRES 7 B 241 GLY GLY GLY ILE ARG SER LEU ASP TYR ALA GLU LYS LEU
SEQRES 8 B 241 ARG LYS LEU GLY TYR ARG ARG GLN ILE VAL SER SER LYS
SEQRES 9 B 241 VAL LEU GLU ASP PRO SER PHE LEU LYS SER LEU ARG GLU
SEQRES 10 B 241 ILE ASP VAL GLU PRO VAL PHE SER LEU ASP THR ARG GLY
SEQRES 11 B 241 GLY ARG VAL ALA PHE LYS GLY TRP LEU ALA GLU GLU GLU
SEQRES 12 B 241 ILE ASP PRO VAL SER LEU LEU LYS ARG LEU LYS GLU TYR
SEQRES 13 B 241 GLY LEU GLU GLU ILE VAL HIS THR GLU ILE GLU LYS ASP
SEQRES 14 B 241 GLY THR LEU GLN GLU HIS ASP PHE SER LEU THR LYS LYS
SEQRES 15 B 241 ILE ALA ILE GLU ALA GLU VAL LYS VAL LEU ALA ALA GLY
SEQRES 16 B 241 GLY ILE SER SER GLU ASN SER LEU LYS THR ALA GLN LYS
SEQRES 17 B 241 VAL HIS THR GLU THR ASN GLY LEU LEU LYS GLY VAL ILE
SEQRES 18 B 241 VAL GLY ARG ALA PHE LEU GLU GLY ILE LEU THR VAL GLU
SEQRES 19 B 241 VAL MSE LYS ARG TYR ALA ARG
MODRES 1QO2 MSE A 1 MET SELENOMETHIONINE
MODRES 1QO2 MSE A 17 MET SELENOMETHIONINE
MODRES 1QO2 MSE A 236 MET SELENOMETHIONINE
MODRES 1QO2 MSE B 1 MET SELENOMETHIONINE
MODRES 1QO2 MSE B 17 MET SELENOMETHIONINE
MODRES 1QO2 MSE B 236 MET SELENOMETHIONINE
HET MSE A 1 8
HET MSE A 17 8
HET MSE A 236 8
HET MSE B 1 8
HET MSE B 17 8
HET MSE B 236 8
HETNAM MSE SELENOMETHIONINE
FORMUL 1 MSE 6(C5 H11 N O2 SE)
FORMUL 3 HOH *547(H2 O)
HELIX 1 1 LYS A 19 GLU A 23 5 5
HELIX 2 2 ASP A 31 GLU A 42 1 12
HELIX 3 3 LEU A 52 ASN A 58 1 7
HELIX 4 4 ASN A 62 LEU A 69 1 8
HELIX 5 5 SER A 70 GLU A 74 5 5
HELIX 6 6 SER A 84 LEU A 94 1 11
HELIX 7 7 SER A 102 ASP A 108 1 7
HELIX 8 8 SER A 110 GLU A 117 1 8
HELIX 9 9 ASP A 145 GLU A 155 1 11
HELIX 10 10 GLU A 167 LEU A 172 1 6
HELIX 11 11 ASP A 176 GLU A 188 1 13
HELIX 12 12 SER A 199 THR A 213 1 15
HELIX 13 13 GLY A 223 GLU A 228 1 6
HELIX 14 14 THR A 232 ARG A 241 1 10
HELIX 15 15 LYS B 19 GLU B 23 5 5
HELIX 16 16 ASP B 31 GLU B 42 1 12
HELIX 17 17 LEU B 52 ASN B 58 1 7
HELIX 18 18 ASN B 62 SER B 70 1 9
HELIX 19 19 GLU B 71 GLU B 74 5 4
HELIX 20 20 SER B 84 GLY B 95 1 12
HELIX 21 21 SER B 102 ASP B 108 1 7
HELIX 22 22 SER B 110 ILE B 118 1 9
HELIX 23 23 ASP B 145 GLU B 155 1 11
HELIX 24 24 ASP B 176 GLU B 188 1 13
HELIX 25 25 SER B 199 THR B 213 1 15
HELIX 26 26 GLY B 223 GLU B 228 1 6
HELIX 27 27 THR B 232 TYR B 239 1 8
SHEET 1 A 8 ILE A 76 GLY A 79 0
SHEET 2 A 8 ILE A 47 ASP A 51 1 N ILE A 47 O GLN A 77
SHEET 3 A 8 VAL A 3 LEU A 9 1 N PRO A 5 O HIS A 48
SHEET 4 A 8 LEU A 217 VAL A 222 1 N VAL A 220 O VAL A 4
SHEET 5 A 8 LYS A 190 ALA A 194 1 N VAL A 191 O LYS A 218
SHEET 6 A 8 GLU A 160 GLU A 165 1 N ILE A 161 O LYS A 190
SHEET 7 A 8 GLU A 121 THR A 128 1 N PHE A 124 O GLU A 160
SHEET 8 A 8 ARG A 98 VAL A 101 1 N GLN A 99 O GLU A 121
SHEET 1 B 2 ASP A 8 PHE A 10 0
SHEET 2 B 2 LYS A 13 ALA A 15 -1 N ALA A 15 O ASP A 8
SHEET 1 C 9 VAL B 220 VAL B 222 0
SHEET 2 C 9 VAL B 3 LEU B 9 1 N VAL B 4 O VAL B 220
SHEET 3 C 9 ILE B 47 ASP B 51 1 N HIS B 48 O PRO B 5
SHEET 4 C 9 ILE B 76 GLY B 79 1 N GLN B 77 O ILE B 47
SHEET 5 C 9 ARG B 98 VAL B 101 1 N ARG B 98 O ILE B 78
SHEET 6 C 9 GLU B 121 THR B 128 1 N GLU B 121 O GLN B 99
SHEET 7 C 9 GLU B 160 GLU B 165 1 N VAL B 162 O PHE B 124
SHEET 8 C 9 LYS B 190 ALA B 194 1 N LYS B 190 O ILE B 161
SHEET 9 C 9 LEU B 217 VAL B 220 1 N LYS B 218 O VAL B 191
SHEET 1 D 3 ASP B 8 PHE B 10 0
SHEET 2 D 3 LYS B 13 ARG B 16 -1 N ALA B 15 O ASP B 8
SHEET 3 D 3 ILE B 26 TYR B 28 -1 N TYR B 28 O VAL B 14
LINK C MSE A 1 N LEU A 2 1555 1555 1.33
LINK C ARG A 16 N MSE A 17 1555 1555 1.33
LINK C MSE A 17 N ILE A 18 1555 1555 1.33
LINK C VAL A 235 N MSE A 236 1555 1555 1.33
LINK C MSE A 236 N LYS A 237 1555 1555 1.33
LINK C MSE B 1 N LEU B 2 1555 1555 1.33
LINK C ARG B 16 N MSE B 17 1555 1555 1.33
LINK C MSE B 17 N ILE B 18 1555 1555 1.33
LINK C VAL B 235 N MSE B 236 1555 1555 1.33
LINK C MSE B 236 N LYS B 237 1555 1555 1.33
CRYST1 46.780 73.160 62.700 90.00 97.42 90.00 P 1 21 1 4
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 0.021377 0.000000 0.002784 0.00000
SCALE2 0.000000 0.013669 0.000000 0.00000
SCALE3 0.000000 0.000000 0.016084 0.00000
MTRIX1 1 -0.999200 -0.012980 -0.037910 16.28184 1
MTRIX2 1 -0.038510 0.050160 0.998000 -4.59496 1
MTRIX3 1 -0.011050 0.998660 -0.050620 5.49976 1
HETATM 1 N MSE A 1 4.180 1.199 40.514 1.00 21.00 N
HETATM 2 CA MSE A 1 2.974 1.126 39.639 1.00 19.30 C
HETATM 3 C MSE A 1 3.354 0.485 38.311 1.00 17.52 C
HETATM 4 O MSE A 1 4.500 0.097 38.102 1.00 16.39 O
HETATM 5 CB MSE A 1 2.420 2.530 39.382 1.00 21.06 C
HETATM 6 CG MSE A 1 3.382 3.438 38.632 1.00 23.41 C
HETATM 7 SE MSE A 1 2.654 5.171 38.171 1.00 26.09 SE
HETATM 8 CE MSE A 1 3.898 5.645 36.770 1.00 25.03 C
(ATOM LINES ARE NOT SHOWN.)
END
