HEADER OXIDOREDUCTASE 09-NOV-00 1G77
TITLE X-RAY STRUCTURE OF ESCHERICHIA COLI PYRIDOXINE 5`-PHOSPHATE OXIDASE
TITLE 2 COMPLEXED WITH PYRIDOXAL 5'-PHOSPHATE AT 2.0 A RESOLUTION
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PYRIDOXINE 5`-PHOSPHATE OXIDASE;
COMPND 3 CHAIN: A;
COMPND 4 EC: 1.4.3.5;
COMPND 5 ENGINEERED: 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;
SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: PET22B
KEYWDS PLP COMPLEX, FMN COMPLEX, PYRIDOXINE 5'-PHOSPHATE, OXIDOREDUCTASE
EXPDTA X-RAY DIFFRACTION
AUTHOR M.K.SAFO,F.N.MUSAYEV,M.L.DI SALVO,V.SCHIRCH
REVDAT 5 13-JUL-11 1G77 1 VERSN
REVDAT 4 24-FEB-09 1G77 1 VERSN
REVDAT 3 01-APR-03 1G77 1 JRNL
REVDAT 2 25-JUL-01 1G77 1 JRNL
REVDAT 1 29-NOV-00 1G77 0
JRNL AUTH M.K.SAFO,F.N.MUSAYEV,M.L.DI SALVO,V.SCHIRCH
JRNL TITL X-RAY STRUCTURE OF ESCHERICHIA COLI PYRIDOXINE 5'-PHOSPHATE
JRNL TITL 2 OXIDASE COMPLEXED WITH PYRIDOXAL 5'-PHOSPHATE AT 2.0 A
JRNL TITL 3 RESOLUTION.
JRNL REF J.MOL.BIOL. V. 310 817 2001
JRNL REFN ISSN 0022-2836
JRNL PMID 11453690
JRNL DOI 10.1006/JMBI.2001.4734
REMARK 2
REMARK 2 RESOLUTION. 2.10 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 0.5
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 AND HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.10
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 55.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 1.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 53854.880
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 95.3
REMARK 3 NUMBER OF REFLECTIONS : 16766
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) : 0.209
REMARK 3 FREE R VALUE : 0.236
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.200
REMARK 3 FREE R VALUE TEST SET COUNT : 872
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.008
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) : 2.10
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.23
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 90.80
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 2455
REMARK 3 BIN R VALUE (WORKING SET) : 0.2650
REMARK 3 BIN FREE R VALUE : 0.2540
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5.50
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 143
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.021
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1642
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 57
REMARK 3 SOLVENT ATOMS : 98
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 17.90
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 29.90
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 3.91000
REMARK 3 B22 (A**2) : 3.91000
REMARK 3 B33 (A**2) : -7.83000
REMARK 3 B12 (A**2) : 4.67000
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) : 0.24
REMARK 3 ESD FROM SIGMAA (A) : 0.25
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) : 0.26
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.22
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.012
REMARK 3 BOND ANGLES (DEGREES) : 1.50
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 23.20
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.89
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) : 1.550 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 2.320 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 2.340 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 3.360 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.38
REMARK 3 BSOL : 48.46
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 : PHOSPHATE.PARAM
REMARK 3 PARAMETER FILE 3 : FMN.PARAM
REMARK 3 PARAMETER FILE 4 : PLP.PARAM
REMARK 3 PARAMETER FILE 5 : &_1_PARAMETER_INFILE_6
REMARK 3 PARAMETER FILE 6 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : WATER.TOP
REMARK 3 TOPOLOGY FILE 3 : FMN.TOP
REMARK 3 TOPOLOGY FILE 4 : PHOSPHATE.TOP
REMARK 3 TOPOLOGY FILE 5 : PLP.TOP
REMARK 3 TOPOLOGY FILE 6 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: BULK SOLVENT CORRECTION
REMARK 4
REMARK 4 1G77 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 10-NOV-00.
REMARK 100 THE RCSB ID CODE IS RCSB012319.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 23-MAR-00
REMARK 200 TEMPERATURE (KELVIN) : 98
REMARK 200 PH : 7.0
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 : RIGAKU RU200
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : L
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : MSC MIRRORS
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS II
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : BIOTEX
REMARK 200 DATA SCALING SOFTWARE : BIOTEX
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 17276
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.100
REMARK 200 RESOLUTION RANGE LOW (A) : 55.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.1
REMARK 200 DATA REDUNDANCY : 3.700
REMARK 200 R MERGE (I) : 0.04900
REMARK 200 R SYM (I) : 5.60000
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 10.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.10
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.33
REMARK 200 COMPLETENESS FOR SHELL (%) : 96.5
REMARK 200 DATA REDUNDANCY IN SHELL : 3.20
REMARK 200 R MERGE FOR SHELL (I) : 0.15600
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.000
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: LAUE
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: FOURIER SYNTHESIS
REMARK 200 SOFTWARE USED: CNS
REMARK 200 STARTING MODEL: PDB ENTRY 1DNL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 56.12
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.80
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: AMMONIUM FORMATE AND MES, PH 7.0,
REMARK 280 VAPOR DIFFUSION, HANGING 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 41.54667
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 83.09333
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 83.09333
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 41.54667
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, WHICH WAS CONSTRUCTUED
REMARK 300 FROM CHAIN A AND ITS SYMMETRY PARTNER GENERATED BY THE TWO-FOLD AXIS
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: 9220 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 17100 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -44.0 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 95.16000
REMARK 350 BIOMT2 2 -0.866025 0.500000 0.000000 54.94065
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 41.54667
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 MSE A 1
REMARK 465 SER A 2
REMARK 465 ASP A 3
REMARK 465 ASN A 4
REMARK 465 ASP A 5
REMARK 465 GLU A 6
REMARK 465 LEU A 7
REMARK 465 GLN A 8
REMARK 465 GLN A 9
REMARK 465 ILE A 10
REMARK 465 ALA A 11
REMARK 465 HIS A 12
REMARK 465 LEU A 13
REMARK 465 ARG A 14
REMARK 465 ARG A 15
REMARK 465 GLU A 16
REMARK 465 TYR A 17
REMARK 465 THR A 18
REMARK 465 LYS A 19
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 NE2 GLN A 66 NE2 GLN A 66 6765 2.08
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 ASP A 49 70.93 43.03
REMARK 500 TRP A 105 32.36 -96.76
REMARK 500 GLN A 146 125.85 -30.81
REMARK 500 SER A 147 -17.63 81.39
REMARK 500 GLN A 168 -7.90 76.82
REMARK 500 GLU A 171 -8.37 -172.60
REMARK 500 VAL A 172 98.12 45.55
REMARK 500 ASN A 208 73.65 74.81
REMARK 500 ASP A 209 -43.16 80.90
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 ARG A 133 0.17 SIDE CHAIN
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 PO4 A 280
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 290
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMN A 250
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PLP A 260
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1G76 RELATED DB: PDB
REMARK 900 1G76 CONTAINS THE SAME PROTEIN COMPLEXED WITH THE SAME
REMARK 900 LIGAND. HOWEVER, THE NUMBER OF BOUND LIGANDS DIFFER.
DBREF 1G77 A 1 218 UNP P28225 PDXH_ECOLI 1 218
SEQADV 1G77 MSE A 1 UNP P28225 MET 0 MODIFIED RESIDUE
SEQADV 1G77 MSE A 53 UNP P28225 MET 52 MODIFIED RESIDUE
SEQADV 1G77 MSE A 79 UNP P28225 MET 78 MODIFIED RESIDUE
SEQADV 1G77 MSE A 113 UNP P28225 MET 112 MODIFIED RESIDUE
SEQADV 1G77 MSE A 127 UNP P28225 MET 126 MODIFIED RESIDUE
SEQRES 1 A 218 MSE SER ASP ASN ASP GLU LEU GLN GLN ILE ALA HIS LEU
SEQRES 2 A 218 ARG ARG GLU TYR THR LYS GLY GLY LEU ARG ARG ARG ASP
SEQRES 3 A 218 LEU PRO ALA ASP PRO LEU THR LEU PHE GLU ARG TRP LEU
SEQRES 4 A 218 SER GLN ALA CYS GLU ALA LYS LEU ALA ASP PRO THR ALA
SEQRES 5 A 218 MSE VAL VAL ALA THR VAL ASP GLU HIS GLY GLN PRO TYR
SEQRES 6 A 218 GLN ARG ILE VAL LEU LEU LYS HIS TYR ASP GLU LYS GLY
SEQRES 7 A 218 MSE VAL PHE TYR THR ASN LEU GLY SER ARG LYS ALA HIS
SEQRES 8 A 218 GLN ILE GLU ASN ASN PRO ARG VAL SER LEU LEU PHE PRO
SEQRES 9 A 218 TRP HIS THR LEU GLU ARG GLN VAL MSE VAL ILE GLY LYS
SEQRES 10 A 218 ALA GLU ARG LEU SER THR LEU GLU VAL MSE LYS TYR PHE
SEQRES 11 A 218 HIS SER ARG PRO ARG ASP SER GLN ILE GLY ALA TRP VAL
SEQRES 12 A 218 SER LYS GLN SER SER ARG ILE SER ALA ARG GLY ILE LEU
SEQRES 13 A 218 GLU SER LYS PHE LEU GLU LEU LYS GLN LYS PHE GLN GLN
SEQRES 14 A 218 GLY GLU VAL PRO LEU PRO SER PHE TRP GLY GLY PHE ARG
SEQRES 15 A 218 VAL SER LEU GLU GLN ILE GLU PHE TRP GLN GLY GLY GLU
SEQRES 16 A 218 HIS ARG LEU HIS ASP ARG PHE LEU TYR GLN ARG GLU ASN
SEQRES 17 A 218 ASP ALA TRP LYS ILE ASP ARG LEU ALA PRO
MODRES 1G77 MSE A 53 MET SELENOMETHIONINE
MODRES 1G77 MSE A 79 MET SELENOMETHIONINE
MODRES 1G77 MSE A 113 MET SELENOMETHIONINE
MODRES 1G77 MSE A 127 MET SELENOMETHIONINE
HET MSE A 53 8
HET MSE A 79 8
HET MSE A 113 8
HET MSE A 127 11
HET PO4 A 280 5
HET PO4 A 290 5
HET FMN A 250 31
HET PLP A 260 16
HETNAM MSE SELENOMETHIONINE
HETNAM PO4 PHOSPHATE ION
HETNAM FMN FLAVIN MONONUCLEOTIDE
HETNAM PLP PYRIDOXAL-5'-PHOSPHATE
HETSYN FMN RIBOFLAVIN MONOPHOSPHATE
HETSYN PLP VITAMIN B6 PHOSPHATE
FORMUL 1 MSE 4(C5 H11 N O2 SE)
FORMUL 2 PO4 2(O4 P 3-)
FORMUL 4 FMN C17 H21 N4 O9 P
FORMUL 5 PLP C8 H10 N O6 P
FORMUL 6 HOH *98(H2 O)
HELIX 1 1 ARG A 23 LEU A 27 5 5
HELIX 2 2 ASP A 30 ALA A 45 1 16
HELIX 3 3 SER A 87 ASN A 96 1 10
HELIX 4 4 HIS A 106 LEU A 108 5 3
HELIX 5 5 SER A 122 HIS A 131 1 10
HELIX 6 6 PRO A 134 SER A 144 1 11
HELIX 7 7 ALA A 152 GLN A 165 1 14
HELIX 8 8 GLY A 194 LEU A 198 5 5
SHEET 1 A 8 TRP A 211 ARG A 215 0
SHEET 2 A 8 ASP A 200 ARG A 206 -1 N LEU A 203 O ASP A 214
SHEET 3 A 8 TRP A 178 GLN A 192 -1 N ARG A 182 O GLU A 119
SHEET 4 A 8 ARG A 110 ARG A 120 -1 O GLN A 111 N TRP A 191
SHEET 5 A 8 ARG A 98 PHE A 103 -1 N VAL A 99 O GLY A 116
SHEET 6 A 8 ALA A 52 VAL A 58 -1 N VAL A 54 O LEU A 102
SHEET 7 A 8 PRO A 64 ASP A 75 -1 N TYR A 65 O THR A 57
SHEET 8 A 8 GLY A 78 ASN A 84 -1 O MSE A 79 N VAL A 183
LINK C ALA A 52 N MSE A 53 1555 1555 1.33
LINK C MSE A 53 N VAL A 54 1555 1555 1.33
LINK C GLY A 78 N MSE A 79 1555 1555 1.34
LINK C MSE A 79 N VAL A 80 1555 1555 1.33
LINK C VAL A 112 N MSE A 113 1555 1555 1.34
LINK C MSE A 113 N VAL A 114 1555 1555 1.33
LINK C VAL A 126 N MSE A 127 1555 1555 1.33
LINK C MSE A 127 N LYS A 128 1555 1555 1.33
SITE 1 AC1 9 ARG A 23 ARG A 24 ARG A 120 ALA A 152
SITE 2 AC1 9 ARG A 153 ARG A 215 HOH A 310 HOH A 329
SITE 3 AC1 9 HOH A 336
SITE 1 AC2 2 SER A 148 ARG A 149
SITE 1 AC3 18 ARG A 67 ILE A 68 VAL A 69 LEU A 70
SITE 2 AC3 18 TYR A 82 THR A 83 SER A 87 ARG A 88
SITE 3 AC3 18 LYS A 89 GLN A 111 GLN A 146 SER A 147
SITE 4 AC3 18 TRP A 191 ARG A 201 PLP A 260 HOH A 308
SITE 5 AC3 18 HOH A 312 HOH A 322
SITE 1 AC4 9 LYS A 72 TYR A 129 ARG A 133 GLN A 146
SITE 2 AC4 9 ARG A 197 HIS A 199 PRO A 218 FMN A 250
SITE 3 AC4 9 HOH A 338
CRYST1 63.440 63.440 124.640 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 0.015763 0.009101 0.000000 0.00000
SCALE2 0.000000 0.018201 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008023 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
