HEADER LYASE 15-MAY-02 1LRO
TITLE AQUIFEX AEOLICUS KDO8P SYNTHASE H185G MUTANT IN COMPLEX WITH PEP AND
TITLE 2 CADMIUM
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: KDO-8-PHOSPHATE SYNTHETASE;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: 2-DEHYDRO-3-DEOXYPHOSPHOOCTONATE ALDOLASE, PHOSPHO-2-
COMPND 5 DEHYDRO-3-DEOXYOCTONATE ALDOLASE, 3-DEOXY-D-MANNO-OCTULOSONIC ACID 8-
COMPND 6 PHOSPHATE SYNTHETASE, KDO 8-P SYNTHASE;
COMPND 7 EC: 4.1.2.16;
COMPND 8 ENGINEERED: YES;
COMPND 9 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: AQUIFEX AEOLICUS;
SOURCE 3 ORGANISM_TAXID: 63363;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: PAAKDSA
KEYWDS KDO8PS, KDO8P, KDO, LYASE
EXPDTA X-RAY DIFFRACTION
AUTHOR J.WANG,H.S.DUEWEL,J.A.STUCKEY,R.W.WOODARD,D.L.GATTI
REVDAT 6 14-FEB-24 1LRO 1 REMARK
REVDAT 5 27-OCT-21 1LRO 1 REMARK SEQADV LINK
REVDAT 4 11-OCT-17 1LRO 1 REMARK
REVDAT 3 13-JUL-11 1LRO 1 VERSN
REVDAT 2 24-FEB-09 1LRO 1 VERSN
REVDAT 1 27-NOV-02 1LRO 0
JRNL AUTH J.WANG,H.S.DUEWEL,J.A.STUCKEY,R.W.WOODARD,D.L.GATTI
JRNL TITL FUNCTION OF HIS185 IN AQUIFEX AEOLICUS
JRNL TITL 2 3-DEOXY-D-MANNO-OCTULOSONATE 8-PHOSPHATE SYNTHASE
JRNL REF J.MOL.BIOL. V. 324 205 2002
JRNL REFN ISSN 0022-2836
JRNL PMID 12441100
JRNL DOI 10.1016/S0022-2836(02)01096-3
REMARK 2
REMARK 2 RESOLUTION. 1.80 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.0
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) : 1.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.29
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 97.0
REMARK 3 NUMBER OF REFLECTIONS : 60254
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) : 0.207
REMARK 3 FREE R VALUE : 0.230
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 10.200
REMARK 3 FREE R VALUE TEST SET COUNT : 6140
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 : 6
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.80
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.91
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 92.20
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 8428
REMARK 3 BIN R VALUE (WORKING SET) : 0.3250
REMARK 3 BIN FREE R VALUE : 0.3590
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 10.40
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 976
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.011
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4031
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 32
REMARK 3 SOLVENT ATOMS : 271
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 30.60
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 33.30
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 3.92000
REMARK 3 B22 (A**2) : 3.92000
REMARK 3 B33 (A**2) : -7.85000
REMARK 3 B12 (A**2) : 3.00000
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) : 0.22
REMARK 3 ESD FROM SIGMAA (A) : 0.19
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) : 0.25
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.20
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.006
REMARK 3 BOND ANGLES (DEGREES) : 1.300
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 22.40
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.780
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) : 1.180 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 1.790 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 1.900 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 2.830 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.39
REMARK 3 BSOL : 53.78
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 : ION.PARAM
REMARK 3 PARAMETER FILE 4 : PEP_A5P_MOD4
REMARK 3 PARAMETER FILE 5 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : WATER.TOP
REMARK 3 TOPOLOGY FILE 3 : ION.TOP
REMARK 3 TOPOLOGY FILE 4 : PEP_A5P.TOPH
REMARK 3 TOPOLOGY FILE 5 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1LRO COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 16-MAY-02.
REMARK 100 THE DEPOSITION ID IS D_1000016223.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 03-DEC-01
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 4.8
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) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : MIRROR
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : R-AXIS
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 60254
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.800
REMARK 200 RESOLUTION RANGE LOW (A) : 20.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.0
REMARK 200 DATA REDUNDANCY : 8.900
REMARK 200 R MERGE (I) : 0.12000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 10.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.80
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.91
REMARK 200 COMPLETENESS FOR SHELL (%) : 92.2
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: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 55.79
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.78
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM NA-ACETATE 6% PEG 4000, PH 4.8,
REMARK 280 VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 278K
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 53.52700
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 107.05400
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 107.05400
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 53.52700
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 TETRAMER CONSTRUCTED FROM
REMARK 300 CHAIN A AND CHAIN B AND THEIR SYMMETRY PARTNERS GENERATED BY
REMARK 300 APPLICATION OF THE SYMMETRY OPERATION (X=Y, Y=X, Z=-Z)
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: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA,PQS
REMARK 350 TOTAL BURIED SURFACE AREA: 16320 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 33790 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -124.0 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 350 BIOMT1 2 -0.500000 0.866025 0.000000 0.00000
REMARK 350 BIOMT2 2 0.866025 0.500000 0.000000 0.00000
REMARK 350 BIOMT3 2 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 MET A 1001
REMARK 465 GLY A 1194
REMARK 465 ASP A 1195
REMARK 465 LYS A 1196
REMARK 465 SER A 1197
REMARK 465 PRO A 1265
REMARK 465 VAL A 1266
REMARK 465 LYS A 1267
REMARK 465 MET B 2001
REMARK 465 GLU B 2002
REMARK 465 GLY B 2192
REMARK 465 LEU B 2193
REMARK 465 GLY B 2194
REMARK 465 ASP B 2195
REMARK 465 LYS B 2196
REMARK 465 SER B 2197
REMARK 465 GLY B 2198
REMARK 465 ILE B 2264
REMARK 465 PRO B 2265
REMARK 465 VAL B 2266
REMARK 465 LYS B 2267
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 GLU A1072 CD GLU A1072 OE2 0.076
REMARK 500 GLY B2191 C GLY B2191 O 0.198
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 SER A1042 140.65 -171.34
REMARK 500 SER B2015 153.23 173.62
REMARK 500 PHE B2033 75.22 -110.66
REMARK 500 SER B2042 149.22 -173.21
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CD A1270 CD
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A1011 SG
REMARK 620 2 GLU A1222 OE2 97.1
REMARK 620 3 GLU A1222 OE1 107.4 54.4
REMARK 620 4 ASP A1233 OD2 102.3 148.0 95.2
REMARK 620 5 PEP A1268 O2' 136.3 79.1 105.2 102.9
REMARK 620 6 PEP A1268 O1 91.5 111.7 157.1 93.1 52.1
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CD B2270 CD
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS B2011 SG
REMARK 620 2 GLU B2222 OE1 104.5
REMARK 620 3 GLU B2222 OE2 96.5 54.5
REMARK 620 4 ASP B2233 OD2 101.6 97.2 149.8
REMARK 620 5 PEP B2268 O2' 135.3 112.9 86.5 97.2
REMARK 620 6 PEP B2268 O1 88.0 164.2 115.4 89.5 51.8
REMARK 620 N 1 2 3 4 5
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 1269
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 B 2269
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CD A 1270
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CD B 2270
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEP A 1268
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEP B 2268
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1FWW RELATED DB: PDB
REMARK 900 AQUIFEX AEOLICUS KDO8P SYNTHASE IN COMPLEX WITH PEP, A5P AND CADMIUM
REMARK 900 RELATED ID: 1LRN RELATED DB: PDB
REMARK 900 AQUIFEX AEOLICUS KDO8P SYNTHASE H185G MUTANT IN COMPLEX WITH CADMIUM
REMARK 900 RELATED ID: 1LRQ RELATED DB: PDB
REMARK 900 AQUIFEX AEOLICUS KDO8P SYNTHASE H185G MUTANT IN COMPLEX WITH PEP,
REMARK 900 A5P AND CADMIUM
DBREF 1LRO A 1001 1267 UNP O66496 KDSA_AQUAE 1 267
DBREF 1LRO B 2001 2267 UNP O66496 KDSA_AQUAE 1 267
SEQADV 1LRO GLY A 1185 UNP O66496 HIS 185 ENGINEERED MUTATION
SEQADV 1LRO GLY B 2185 UNP O66496 HIS 185 ENGINEERED MUTATION
SEQRES 1 A 267 MET GLU LYS PHE LEU VAL ILE ALA GLY PRO CYS ALA ILE
SEQRES 2 A 267 GLU SER GLU GLU LEU LEU LEU LYS VAL GLY GLU GLU ILE
SEQRES 3 A 267 LYS ARG LEU SER GLU LYS PHE LYS GLU VAL GLU PHE VAL
SEQRES 4 A 267 PHE LYS SER SER PHE ASP LYS ALA ASN ARG SER SER ILE
SEQRES 5 A 267 HIS SER PHE ARG GLY HIS GLY LEU GLU TYR GLY VAL LYS
SEQRES 6 A 267 ALA LEU ARG LYS VAL LYS GLU GLU PHE GLY LEU LYS ILE
SEQRES 7 A 267 THR THR ASP ILE HIS GLU SER TRP GLN ALA GLU PRO VAL
SEQRES 8 A 267 ALA GLU VAL ALA ASP ILE ILE GLN ILE PRO ALA PHE LEU
SEQRES 9 A 267 CYS ARG GLN THR ASP LEU LEU LEU ALA ALA ALA LYS THR
SEQRES 10 A 267 GLY ARG ALA VAL ASN VAL LYS LYS GLY GLN PHE LEU ALA
SEQRES 11 A 267 PRO TRP ASP THR LYS ASN VAL VAL GLU LYS LEU LYS PHE
SEQRES 12 A 267 GLY GLY ALA LYS GLU ILE TYR LEU THR GLU ARG GLY THR
SEQRES 13 A 267 THR PHE GLY TYR ASN ASN LEU VAL VAL ASP PHE ARG SER
SEQRES 14 A 267 LEU PRO ILE MET LYS GLN TRP ALA LYS VAL ILE TYR ASP
SEQRES 15 A 267 ALA THR GLY SER VAL GLN LEU PRO GLY GLY LEU GLY ASP
SEQRES 16 A 267 LYS SER GLY GLY MET ARG GLU PHE ILE PHE PRO LEU ILE
SEQRES 17 A 267 ARG ALA ALA VAL ALA VAL GLY CYS ASP GLY VAL PHE MET
SEQRES 18 A 267 GLU THR HIS PRO GLU PRO GLU LYS ALA LEU SER ASP ALA
SEQRES 19 A 267 SER THR GLN LEU PRO LEU SER GLN LEU GLU GLY ILE ILE
SEQRES 20 A 267 GLU ALA ILE LEU GLU ILE ARG GLU VAL ALA SER LYS TYR
SEQRES 21 A 267 TYR GLU THR ILE PRO VAL LYS
SEQRES 1 B 267 MET GLU LYS PHE LEU VAL ILE ALA GLY PRO CYS ALA ILE
SEQRES 2 B 267 GLU SER GLU GLU LEU LEU LEU LYS VAL GLY GLU GLU ILE
SEQRES 3 B 267 LYS ARG LEU SER GLU LYS PHE LYS GLU VAL GLU PHE VAL
SEQRES 4 B 267 PHE LYS SER SER PHE ASP LYS ALA ASN ARG SER SER ILE
SEQRES 5 B 267 HIS SER PHE ARG GLY HIS GLY LEU GLU TYR GLY VAL LYS
SEQRES 6 B 267 ALA LEU ARG LYS VAL LYS GLU GLU PHE GLY LEU LYS ILE
SEQRES 7 B 267 THR THR ASP ILE HIS GLU SER TRP GLN ALA GLU PRO VAL
SEQRES 8 B 267 ALA GLU VAL ALA ASP ILE ILE GLN ILE PRO ALA PHE LEU
SEQRES 9 B 267 CYS ARG GLN THR ASP LEU LEU LEU ALA ALA ALA LYS THR
SEQRES 10 B 267 GLY ARG ALA VAL ASN VAL LYS LYS GLY GLN PHE LEU ALA
SEQRES 11 B 267 PRO TRP ASP THR LYS ASN VAL VAL GLU LYS LEU LYS PHE
SEQRES 12 B 267 GLY GLY ALA LYS GLU ILE TYR LEU THR GLU ARG GLY THR
SEQRES 13 B 267 THR PHE GLY TYR ASN ASN LEU VAL VAL ASP PHE ARG SER
SEQRES 14 B 267 LEU PRO ILE MET LYS GLN TRP ALA LYS VAL ILE TYR ASP
SEQRES 15 B 267 ALA THR GLY SER VAL GLN LEU PRO GLY GLY LEU GLY ASP
SEQRES 16 B 267 LYS SER GLY GLY MET ARG GLU PHE ILE PHE PRO LEU ILE
SEQRES 17 B 267 ARG ALA ALA VAL ALA VAL GLY CYS ASP GLY VAL PHE MET
SEQRES 18 B 267 GLU THR HIS PRO GLU PRO GLU LYS ALA LEU SER ASP ALA
SEQRES 19 B 267 SER THR GLN LEU PRO LEU SER GLN LEU GLU GLY ILE ILE
SEQRES 20 B 267 GLU ALA ILE LEU GLU ILE ARG GLU VAL ALA SER LYS TYR
SEQRES 21 B 267 TYR GLU THR ILE PRO VAL LYS
HET PO4 A1269 5
HET CD A1270 1
HET PEP A1268 10
HET PO4 B2269 5
HET CD B2270 1
HET PEP B2268 10
HETNAM PO4 PHOSPHATE ION
HETNAM CD CADMIUM ION
HETNAM PEP PHOSPHOENOLPYRUVATE
FORMUL 3 PO4 2(O4 P 3-)
FORMUL 4 CD 2(CD 2+)
FORMUL 5 PEP 2(C3 H5 O6 P)
FORMUL 9 HOH *271(H2 O)
HELIX 1 1 SER A 1015 PHE A 1033 1 19
HELIX 2 2 GLY A 1059 GLY A 1075 1 17
HELIX 3 3 GLU A 1084 TRP A 1086 5 3
HELIX 4 4 GLN A 1087 GLU A 1093 1 7
HELIX 5 5 PRO A 1101 CYS A 1105 5 5
HELIX 6 6 GLN A 1107 LYS A 1116 1 10
HELIX 7 7 ALA A 1130 ASP A 1133 5 4
HELIX 8 8 THR A 1134 GLY A 1144 1 11
HELIX 9 9 ARG A 1168 LYS A 1174 1 7
HELIX 10 10 THR A 1184 GLN A 1188 5 5
HELIX 11 11 MET A 1200 GLU A 1202 5 3
HELIX 12 12 PHE A 1203 GLY A 1215 1 13
HELIX 13 13 GLU A 1226 ALA A 1230 5 5
HELIX 14 14 GLN A 1242 LYS A 1259 1 18
HELIX 15 15 SER B 2015 PHE B 2033 1 19
HELIX 16 16 GLY B 2059 GLY B 2075 1 17
HELIX 17 17 GLU B 2084 TRP B 2086 5 3
HELIX 18 18 GLN B 2087 ALA B 2092 1 6
HELIX 19 19 PRO B 2101 CYS B 2105 5 5
HELIX 20 20 GLN B 2107 THR B 2117 1 11
HELIX 21 21 ALA B 2130 ASP B 2133 5 4
HELIX 22 22 THR B 2134 GLY B 2144 1 11
HELIX 23 23 ARG B 2168 LYS B 2174 1 7
HELIX 24 24 MET B 2200 GLU B 2202 5 3
HELIX 25 25 PHE B 2203 GLY B 2215 1 13
HELIX 26 26 GLU B 2226 ALA B 2230 5 5
HELIX 27 27 GLN B 2242 SER B 2258 1 17
HELIX 28 28 LYS B 2259 TYR B 2261 5 3
SHEET 1 A10 LEU A1238 PRO A1239 0
SHEET 2 A10 GLY A1218 HIS A1224 1 O GLU A1222 N LEU A1238
SHEET 3 A10 PHE A1004 GLY A1009 1 O LEU A1005 N VAL A1219
SHEET 4 A10 VAL A1036 LYS A1041 1 N GLU A1037 O PHE A1004
SHEET 5 A10 LYS A1077 ASP A1081 1 O LYS A1077 N PHE A1040
SHEET 6 A10 ILE A1097 ILE A1100 1 N ILE A1097 O ILE A1078
SHEET 7 A10 ALA A1120 LYS A1124 1 O ALA A1120 N ILE A1098
SHEET 8 A10 ILE A1149 GLU A1153 1 N TYR A1150 O VAL A1121
SHEET 9 A10 LYS A1178 ASP A1182 1 O LYS A1178 N LEU A1151
SHEET 10 A10 GLY A1218 HIS A1224 1 O GLY A1218 N TYR A1181
SHEET 1 B 2 THR A1156 THR A1157 0
SHEET 2 B 2 LEU A1163 VAL A1164 -1 N VAL A1164 O THR A1156
SHEET 1 C10 LEU B2238 PRO B2239 0
SHEET 2 C10 GLY B2218 HIS B2224 1 O GLU B2222 N LEU B2238
SHEET 3 C10 LEU B2005 GLY B2009 1 O LEU B2005 N VAL B2219
SHEET 4 C10 GLU B2037 LYS B2041 1 O GLU B2037 N VAL B2006
SHEET 5 C10 LYS B2077 ASP B2081 1 O LYS B2077 N PHE B2040
SHEET 6 C10 ILE B2097 ILE B2100 1 N ILE B2097 O ILE B2078
SHEET 7 C10 ALA B2120 LYS B2124 1 O ALA B2120 N ILE B2098
SHEET 8 C10 ILE B2149 GLU B2153 1 O TYR B2150 N VAL B2123
SHEET 9 C10 LYS B2178 ASP B2182 1 O LYS B2178 N LEU B2151
SHEET 10 C10 GLY B2218 HIS B2224 1 O GLY B2218 N TYR B2181
SHEET 1 D 2 THR B2156 THR B2157 0
SHEET 2 D 2 LEU B2163 VAL B2164 -1 O VAL B2164 N THR B2156
LINK SG CYS A1011 CD CD A1270 1555 1555 2.37
LINK OE2 GLU A1222 CD CD A1270 1555 1555 2.62
LINK OE1 GLU A1222 CD CD A1270 1555 1555 2.08
LINK OD2 ASP A1233 CD CD A1270 1555 1555 1.89
LINK O2' PEP A1268 CD CD A1270 1555 1555 2.42
LINK O1 PEP A1268 CD CD A1270 1555 1555 2.52
LINK SG CYS B2011 CD CD B2270 1555 1555 2.46
LINK OE1 GLU B2222 CD CD B2270 1555 1555 2.14
LINK OE2 GLU B2222 CD CD B2270 1555 1555 2.59
LINK OD2 ASP B2233 CD CD B2270 1555 1555 1.98
LINK O2' PEP B2268 CD CD B2270 1555 1555 2.29
LINK O1 PEP B2268 CD CD B2270 1555 1555 2.64
SITE 1 AC1 3 HOH A 32 ARG A1049 SER A1050
SITE 1 AC2 6 ARG A1106 HOH B 44 HOH B 180 HOH B 275
SITE 2 AC2 6 ARG B2049 SER B2050
SITE 1 AC3 4 CYS A1011 GLU A1222 ASP A1233 PEP A1268
SITE 1 AC4 4 CYS B2011 GLU B2222 ASP B2233 PEP B2268
SITE 1 AC5 14 HOH A 21 HOH A 39 HOH A 91 HOH A 93
SITE 2 AC5 14 HOH A 233 CYS A1011 LYS A1046 PRO A1101
SITE 3 AC5 14 ALA A1102 LYS A1124 ARG A1154 GLU A1222
SITE 4 AC5 14 ASP A1233 CD A1270
SITE 1 AC6 14 HOH B 27 HOH B 59 HOH B 61 HOH B 108
SITE 2 AC6 14 HOH B 127 CYS B2011 LYS B2046 PRO B2101
SITE 3 AC6 14 ALA B2102 LYS B2124 ARG B2154 GLU B2222
SITE 4 AC6 14 ASP B2233 CD B2270
CRYST1 84.450 84.450 160.581 90.00 90.00 120.00 P 31 2 1 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 0.011841 0.006837 0.000000 0.00000
SCALE2 0.000000 0.013673 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006227 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
