HEADER ISOMERASE 19-SEP-05 2B2K
TITLE STRUCTURE OF Y104F IDI-1 MUTANT IN COMPLEX WITH EIPP
CAVEAT 2B2K CHIRALITY ERROR AT C12 OF EIP 401 IN CHAIN A, B.
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ISOPENTENYL-DIPHOSPHATE DELTA-ISOMERASE;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: DIMETHYLALLYL DIPHOSPHATE ISOMERASE, IPP ISOMERASE,
COMPND 5 ISOPENTENYL PYROPHOSPHATE ISOMERASE, IPP:DMAPP ISOMERASE;
COMPND 6 EC: 5.3.3.2;
COMPND 7 ENGINEERED: YES;
COMPND 8 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;
SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: PYL20
KEYWDS COMPLEX, ISOMERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR J.WOUTERS
REVDAT 6 25-OCT-23 2B2K 1 REMARK
REVDAT 5 10-NOV-21 2B2K 1 REMARK SEQADV LINK
REVDAT 4 26-OCT-11 2B2K 1 CAVEAT
REVDAT 3 19-OCT-11 2B2K 1 REMARK VERSN
REVDAT 2 24-FEB-09 2B2K 1 VERSN
REVDAT 1 05-SEP-06 2B2K 0
JRNL AUTH J.DE RUYCK,V.DURISOTTI,Y.OUDJAMA,J.WOUTERS
JRNL TITL STRUCTURAL ROLE FOR TYR-104 IN ESCHERICHIA COLI
JRNL TITL 2 ISOPENTENYL-DIPHOSPHATE ISOMERASE: SITE-DIRECTED
JRNL TITL 3 MUTAGENESIS, ENZYMOLOGY, AND PROTEIN CRYSTALLOGRAPHY
JRNL REF J.BIOL.CHEM. V. 281 17864 2006
JRNL REFN ISSN 0021-9258
JRNL PMID 16617181
JRNL DOI 10.1074/JBC.M601851200
REMARK 2
REMARK 2 RESOLUTION. 1.97 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : SHELXL-97
REMARK 3 AUTHORS : G.M.SHELDRICK
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.97
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 8.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 4.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 90.0
REMARK 3 CROSS-VALIDATION METHOD : FREE R
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (NO CUTOFF).
REMARK 3 R VALUE (WORKING + TEST SET, NO CUTOFF) : 0.215
REMARK 3 R VALUE (WORKING SET, NO CUTOFF) : 0.215
REMARK 3 FREE R VALUE (NO CUTOFF) : 0.245
REMARK 3 FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : 10.000
REMARK 3 FREE R VALUE TEST SET COUNT (NO CUTOFF) : 3195
REMARK 3 TOTAL NUMBER OF REFLECTIONS (NO CUTOFF) : 29017
REMARK 3
REMARK 3 FIT/AGREEMENT OF MODEL FOR DATA WITH F>4SIG(F).
REMARK 3 R VALUE (WORKING + TEST SET, F>4SIG(F)) : NULL
REMARK 3 R VALUE (WORKING SET, F>4SIG(F)) : 0.199
REMARK 3 FREE R VALUE (F>4SIG(F)) : 0.229
REMARK 3 FREE R VALUE TEST SET SIZE (%, F>4SIG(F)) : 10.000
REMARK 3 FREE R VALUE TEST SET COUNT (F>4SIG(F)) : 2785
REMARK 3 TOTAL NUMBER OF REFLECTIONS (F>4SIG(F)) : 25339
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2819
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 34
REMARK 3 SOLVENT ATOMS : 106
REMARK 3
REMARK 3 MODEL REFINEMENT.
REMARK 3 OCCUPANCY SUM OF NON-HYDROGEN ATOMS : 2960.0
REMARK 3 OCCUPANCY SUM OF HYDROGEN ATOMS : 0.00
REMARK 3 NUMBER OF DISCRETELY DISORDERED RESIDUES : 0
REMARK 3 NUMBER OF LEAST-SQUARES PARAMETERS : 11843
REMARK 3 NUMBER OF RESTRAINTS : 11788
REMARK 3
REMARK 3 RMS DEVIATIONS FROM RESTRAINT TARGET VALUES.
REMARK 3 BOND LENGTHS (A) : 0.005
REMARK 3 ANGLE DISTANCES (A) : 0.021
REMARK 3 SIMILAR DISTANCES (NO TARGET VALUES) (A) : 0.000
REMARK 3 DISTANCES FROM RESTRAINT PLANES (A) : 0.027
REMARK 3 ZERO CHIRAL VOLUMES (A**3) : 0.028
REMARK 3 NON-ZERO CHIRAL VOLUMES (A**3) : 0.031
REMARK 3 ANTI-BUMPING DISTANCE RESTRAINTS (A) : 0.006
REMARK 3 RIGID-BOND ADP COMPONENTS (A**2) : 0.000
REMARK 3 SIMILAR ADP COMPONENTS (A**2) : 0.075
REMARK 3 APPROXIMATELY ISOTROPIC ADPS (A**2) : 0.000
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED: NULL
REMARK 3
REMARK 3 STEREOCHEMISTRY TARGET VALUES : ENGH & HUBER
REMARK 3 SPECIAL CASE: NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2B2K COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 29-SEP-05.
REMARK 100 THE DEPOSITION ID IS D_1000034596.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 10-MAY-04
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.5
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
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : NI FILTER
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MATHKL, MARHKL
REMARK 200 DATA SCALING SOFTWARE : MATHKL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 25339
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.960
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 (%) : 99.1
REMARK 200 DATA REDUNDANCY : 7.600
REMARK 200 R MERGE (I) : 0.05500
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 16.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.96
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.03
REMARK 200 COMPLETENESS FOR SHELL (%) : 93.4
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.33100
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: SHELX
REMARK 200 STARTING MODEL: 1HX3
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 55.18
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.74
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 2000, MANGANESE CHLORIDE, PH 5.5,
REMARK 280 VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 X+1/2,-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 34.46750
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 45.97750
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 35.73850
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 45.97750
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 34.46750
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 35.73850
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
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
REMARK 350 TOTAL BURIED SURFACE AREA: 3070 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 14980 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -34.0 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 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 1
REMARK 465 GLN A 2
REMARK 465 THR A 3
REMARK 465 GLN A 180
REMARK 465 LEU A 181
REMARK 465 LYS A 182
REMARK 465 LEU A 183
REMARK 465 MET B 1
REMARK 465 GLN B 2
REMARK 465 THR B 3
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 THR A 179 C THR A 179 O 0.171
REMARK 500 LEU B 183 C LEU B 183 O 0.171
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
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,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
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 ATM2 ATM3
REMARK 500 ARG A 30 NE - CZ - NH1 ANGL. DEV. = 3.3 DEGREES
REMARK 500 THR A 179 CA - C - O ANGL. DEV. = -20.7 DEGREES
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 ASN A 10 -168.90 -75.20
REMARK 500 TYR A 99 77.41 -151.40
REMARK 500 ALA B 11 6.08 -67.94
REMARK 500 THR B 26 -153.01 -133.75
REMARK 500 ASP B 28 45.67 -141.27
REMARK 500 TRP B 58 56.90 38.24
REMARK 500 TYR B 99 76.95 -168.01
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 MN A 201 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 25 NE2
REMARK 620 2 HIS A 32 NE2 101.6
REMARK 620 3 HIS A 69 NE2 103.5 96.2
REMARK 620 4 GLU A 114 OE1 79.8 152.2 110.6
REMARK 620 5 GLU A 114 OE2 90.6 92.0 161.8 60.3
REMARK 620 6 GLU A 116 OE2 158.8 95.4 87.1 79.3 76.0
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A 301 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 67 O
REMARK 620 2 GLU A 87 OE2 95.9
REMARK 620 3 EIP A 401 O7 91.7 172.0
REMARK 620 4 EIP A 401 O1 103.0 92.0 83.9
REMARK 620 5 HOH A7021 O 83.9 87.0 96.2 173.1
REMARK 620 6 HOH A7022 O 163.0 80.3 93.1 93.7 79.3
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MN B 201 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS B 25 NE2
REMARK 620 2 HIS B 32 NE2 89.9
REMARK 620 3 HIS B 69 NE2 105.0 113.7
REMARK 620 4 GLU B 114 OE2 85.5 89.4 154.2
REMARK 620 5 GLU B 114 OE1 85.9 144.0 101.9 54.7
REMARK 620 6 GLU B 116 OE2 155.1 90.8 97.4 69.6 79.0
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG B 301 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS B 67 O
REMARK 620 2 GLU B 87 OE2 96.8
REMARK 620 3 EIP B 401 O1 97.1 94.3
REMARK 620 4 EIP B 401 O7 90.0 172.5 81.7
REMARK 620 5 HOH B7023 O 86.2 88.4 175.5 95.3
REMARK 620 6 HOH B7024 O 166.9 80.5 95.9 93.6 81.0
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 MN A 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN B 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EIP A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EIP B 401
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1HX3 RELATED DB: PDB
REMARK 900 METAL BOUND PROTEIN
DBREF 2B2K A 1 182 UNP Q46822 IDI_ECOLI 1 182
DBREF 2B2K B 1 182 UNP Q46822 IDI_ECOLI 1 182
SEQADV 2B2K PHE A 104 UNP Q46822 TYR 104 ENGINEERED MUTATION
SEQADV 2B2K LEU A 183 UNP Q46822 CLONING ARTIFACT
SEQADV 2B2K PHE B 104 UNP Q46822 TYR 104 ENGINEERED MUTATION
SEQADV 2B2K LEU B 183 UNP Q46822 CLONING ARTIFACT
SEQRES 1 A 183 MET GLN THR GLU HIS VAL ILE LEU LEU ASN ALA GLN GLY
SEQRES 2 A 183 VAL PRO THR GLY THR LEU GLU LYS TYR ALA ALA HIS THR
SEQRES 3 A 183 ALA ASP THR ARG LEU HIS LEU ALA PHE SER SER TRP LEU
SEQRES 4 A 183 PHE ASN ALA LYS GLY GLN LEU LEU VAL THR ARG ARG ALA
SEQRES 5 A 183 LEU SER LYS LYS ALA TRP PRO GLY VAL TRP THR ASN SER
SEQRES 6 A 183 VAL CYS GLY HIS PRO GLN LEU GLY GLU SER ASN GLU ASP
SEQRES 7 A 183 ALA VAL ILE ARG ARG CYS ARG TYR GLU LEU GLY VAL GLU
SEQRES 8 A 183 ILE THR PRO PRO GLU SER ILE TYR PRO ASP PHE ARG PHE
SEQRES 9 A 183 ARG ALA THR ASP PRO SER GLY ILE VAL GLU ASN GLU VAL
SEQRES 10 A 183 CYS PRO VAL PHE ALA ALA ARG THR THR SER ALA LEU GLN
SEQRES 11 A 183 ILE ASN ASP ASP GLU VAL MET ASP TYR GLN TRP CYS ASP
SEQRES 12 A 183 LEU ALA ASP VAL LEU HIS GLY ILE ASP ALA THR PRO TRP
SEQRES 13 A 183 ALA PHE SER PRO TRP MET VAL MET GLN ALA THR ASN ARG
SEQRES 14 A 183 GLU ALA ARG LYS ARG LEU SER ALA PHE THR GLN LEU LYS
SEQRES 15 A 183 LEU
SEQRES 1 B 183 MET GLN THR GLU HIS VAL ILE LEU LEU ASN ALA GLN GLY
SEQRES 2 B 183 VAL PRO THR GLY THR LEU GLU LYS TYR ALA ALA HIS THR
SEQRES 3 B 183 ALA ASP THR ARG LEU HIS LEU ALA PHE SER SER TRP LEU
SEQRES 4 B 183 PHE ASN ALA LYS GLY GLN LEU LEU VAL THR ARG ARG ALA
SEQRES 5 B 183 LEU SER LYS LYS ALA TRP PRO GLY VAL TRP THR ASN SER
SEQRES 6 B 183 VAL CYS GLY HIS PRO GLN LEU GLY GLU SER ASN GLU ASP
SEQRES 7 B 183 ALA VAL ILE ARG ARG CYS ARG TYR GLU LEU GLY VAL GLU
SEQRES 8 B 183 ILE THR PRO PRO GLU SER ILE TYR PRO ASP PHE ARG PHE
SEQRES 9 B 183 ARG ALA THR ASP PRO SER GLY ILE VAL GLU ASN GLU VAL
SEQRES 10 B 183 CYS PRO VAL PHE ALA ALA ARG THR THR SER ALA LEU GLN
SEQRES 11 B 183 ILE ASN ASP ASP GLU VAL MET ASP TYR GLN TRP CYS ASP
SEQRES 12 B 183 LEU ALA ASP VAL LEU HIS GLY ILE ASP ALA THR PRO TRP
SEQRES 13 B 183 ALA PHE SER PRO TRP MET VAL MET GLN ALA THR ASN ARG
SEQRES 14 B 183 GLU ALA ARG LYS ARG LEU SER ALA PHE THR GLN LEU LYS
SEQRES 15 B 183 LEU
HET MN A 201 1
HET MG A 301 1
HET EIP A 401 15
HET MN B 201 1
HET MG B 301 1
HET EIP B 401 15
HETNAM MN MANGANESE (II) ION
HETNAM MG MAGNESIUM ION
HETNAM EIP 4-HYDROXY-3-METHYL BUTYL DIPHOSPHATE
FORMUL 3 MN 2(MN 2+)
FORMUL 4 MG 2(MG 2+)
FORMUL 5 EIP 2(C5 H14 O8 P2)
FORMUL 9 HOH *106(H2 O)
HELIX 1 1 LYS A 21 HIS A 25 1 5
HELIX 2 2 SER A 75 GLY A 89 1 15
HELIX 3 3 ASP A 143 THR A 154 1 12
HELIX 4 4 PRO A 155 PHE A 158 5 4
HELIX 5 5 SER A 159 THR A 167 1 9
HELIX 6 6 ASN A 168 SER A 176 1 9
HELIX 7 7 LYS B 21 HIS B 25 1 5
HELIX 8 8 SER B 75 GLY B 89 1 15
HELIX 9 9 ASP B 143 THR B 154 1 12
HELIX 10 10 PRO B 155 PHE B 158 5 4
HELIX 11 11 SER B 159 THR B 167 1 9
HELIX 12 12 ASN B 168 PHE B 178 1 11
SHEET 1 A 2 HIS A 5 LEU A 9 0
SHEET 2 A 2 PRO A 15 GLU A 20 -1 O LEU A 19 N VAL A 6
SHEET 1 B 3 HIS A 32 LEU A 33 0
SHEET 2 B 3 VAL A 113 VAL A 117 1 O VAL A 117 N HIS A 32
SHEET 3 B 3 ARG A 103 THR A 107 -1 N PHE A 104 O GLU A 116
SHEET 1 C 5 TRP A 62 THR A 63 0
SHEET 2 C 5 LEU A 46 ARG A 51 -1 N THR A 49 O THR A 63
SHEET 3 C 5 PHE A 35 PHE A 40 -1 N LEU A 39 O LEU A 47
SHEET 4 C 5 VAL A 120 ARG A 124 1 O PHE A 121 N SER A 36
SHEET 5 C 5 GLU A 96 TYR A 99 -1 N GLU A 96 O ALA A 122
SHEET 1 D 4 VAL A 66 GLY A 68 0
SHEET 2 D 4 PHE A 35 PHE A 40 -1 N PHE A 35 O GLY A 68
SHEET 3 D 4 LEU A 46 ARG A 51 -1 O LEU A 47 N LEU A 39
SHEET 4 D 4 VAL A 136 CYS A 142 -1 O ASP A 138 N ARG A 50
SHEET 1 E 2 HIS B 5 LEU B 9 0
SHEET 2 E 2 PRO B 15 GLU B 20 -1 O LEU B 19 N VAL B 6
SHEET 1 F 3 HIS B 32 LEU B 33 0
SHEET 2 F 3 VAL B 113 VAL B 117 1 O VAL B 117 N HIS B 32
SHEET 3 F 3 ARG B 103 THR B 107 -1 N PHE B 104 O GLU B 116
SHEET 1 G 4 VAL B 66 GLY B 68 0
SHEET 2 G 4 PHE B 35 PHE B 40 -1 N SER B 37 O VAL B 66
SHEET 3 G 4 VAL B 120 ARG B 124 1 O PHE B 121 N SER B 36
SHEET 4 G 4 GLU B 96 TYR B 99 -1 N GLU B 96 O ALA B 122
SHEET 1 H 3 TRP B 62 THR B 63 0
SHEET 2 H 3 LEU B 46 ARG B 51 -1 N THR B 49 O THR B 63
SHEET 3 H 3 VAL B 136 CYS B 142 -1 O CYS B 142 N LEU B 46
LINK OE1 GLU A 116 C12 EIP A 401 1555 1555 1.60
LINK OE1 GLU B 116 C12 EIP B 401 1555 1555 1.60
LINK NE2 HIS A 25 MN MN A 201 1555 1555 2.05
LINK NE2 HIS A 32 MN MN A 201 1555 1555 2.17
LINK O CYS A 67 MG MG A 301 1555 1555 2.15
LINK NE2 HIS A 69 MN MN A 201 1555 1555 1.93
LINK OE2 GLU A 87 MG MG A 301 1555 1555 1.96
LINK OE1 GLU A 114 MN MN A 201 1555 1555 2.12
LINK OE2 GLU A 114 MN MN A 201 1555 1555 2.23
LINK OE2 GLU A 116 MN MN A 201 1555 1555 2.30
LINK MG MG A 301 O7 EIP A 401 1555 1555 1.99
LINK MG MG A 301 O1 EIP A 401 1555 1555 2.09
LINK MG MG A 301 O HOH A7021 1555 1555 1.76
LINK MG MG A 301 O HOH A7022 1555 1555 1.88
LINK NE2 HIS B 25 MN MN B 201 1555 1555 1.89
LINK NE2 HIS B 32 MN MN B 201 1555 1555 1.94
LINK O CYS B 67 MG MG B 301 1555 1555 2.21
LINK NE2 HIS B 69 MN MN B 201 1555 1555 1.99
LINK OE2 GLU B 87 MG MG B 301 1555 1555 2.02
LINK OE2 GLU B 114 MN MN B 201 1555 1555 2.27
LINK OE1 GLU B 114 MN MN B 201 1555 1555 2.41
LINK OE2 GLU B 116 MN MN B 201 1555 1555 2.47
LINK MG MG B 301 O1 EIP B 401 1555 1555 2.01
LINK MG MG B 301 O7 EIP B 401 1555 1555 1.91
LINK MG MG B 301 O HOH B7023 1555 1555 2.12
LINK MG MG B 301 O HOH B7024 1555 1555 2.25
SITE 1 AC1 5 HIS A 25 HIS A 32 HIS A 69 GLU A 114
SITE 2 AC1 5 GLU A 116
SITE 1 AC2 5 HIS B 25 HIS B 32 HIS B 69 GLU B 114
SITE 2 AC2 5 GLU B 116
SITE 1 AC3 5 CYS A 67 GLU A 87 EIP A 401 HOH A7021
SITE 2 AC3 5 HOH A7022
SITE 1 AC4 5 CYS B 67 GLU B 87 EIP B 401 HOH B7023
SITE 2 AC4 5 HOH B7024
SITE 1 AC5 18 LYS A 21 ALA A 34 ARG A 51 LYS A 55
SITE 2 AC5 18 CYS A 67 GLY A 68 HIS A 69 ARG A 83
SITE 3 AC5 18 GLU A 87 GLU A 114 GLU A 116 CYS A 118
SITE 4 AC5 18 MG A 301 HOH A7021 HOH A7022 HOH A7025
SITE 5 AC5 18 HOH A7030 HOH A7038
SITE 1 AC6 16 LYS B 21 ARG B 51 LYS B 55 CYS B 67
SITE 2 AC6 16 GLY B 68 HIS B 69 ARG B 83 GLU B 87
SITE 3 AC6 16 PHE B 104 GLU B 114 GLU B 116 TRP B 161
SITE 4 AC6 16 MG B 301 HOH B7023 HOH B7024 HOH B7031
CRYST1 68.935 71.477 91.955 90.00 90.00 90.00 P 21 21 21 8
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 0.014506 0.000000 0.000000 0.00000
SCALE2 0.000000 0.013991 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010875 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
