HEADER TRANSFERASE 05-MAR-02 1L4U
TITLE CRYSTAL STRUCTURE OF SHIKIMATE KINASE FROM MYCOBACTERIUM TUBERCULOSIS
TITLE 2 IN COMPLEX WITH MGADP AND PT(II) AT 1.8 ANGSTROM RESOLUTION
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SHIKIMATE KINASE;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: SK;
COMPND 5 EC: 2.7.1.71;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MYCOBACTERIUM TUBERCULOSIS;
SOURCE 3 ORGANISM_TAXID: 1773;
SOURCE 4 GENE: AROK;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET-17B
KEYWDS SHIKIMATE PATHWAY, SHIKIMATE KINASE, PHORSPHORYL TRANSFER, DRUG
KEYWDS 2 DESIGN, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR Y.GU,L.RESHETNIKOVA,Y.LI,Y.WU,H.YAN,S.SINGH,X.JI
REVDAT 5 30-AUG-23 1L4U 1 AUTHOR JRNL REMARK LINK
REVDAT 4 29-MAR-17 1L4U 1 VERSN
REVDAT 3 24-FEB-09 1L4U 1 VERSN
REVDAT 2 01-APR-03 1L4U 1 JRNL
REVDAT 1 12-JUN-02 1L4U 0
JRNL AUTH Y.GU,L.RESHETNIKOVA,Y.LI,Y.WU,H.YAN,S.SINGH,X.JI
JRNL TITL CRYSTAL STRUCTURE OF SHIKIMATE KINASE FROM MYCOBACTERIUM
JRNL TITL 2 TUBERCULOSIS REVEALS THE DYNAMIC ROLE OF THE LID DOMAIN IN
JRNL TITL 3 CATALYSIS.
JRNL REF J.MOL.BIOL. V. 319 779 2002
JRNL REFN ISSN 0022-2836
JRNL PMID 12054870
JRNL DOI 10.1016/S0022-2836(02)00339-X
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 : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 272778.210
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 99.7
REMARK 3 NUMBER OF REFLECTIONS : 20594
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) : 0.221
REMARK 3 FREE R VALUE : 0.249
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.900
REMARK 3 FREE R VALUE TEST SET COUNT : 999
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 : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.80
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.83
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.90
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 1029
REMARK 3 BIN R VALUE (WORKING SET) : 0.2750
REMARK 3 BIN FREE R VALUE : 0.3026
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 4.54
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 49
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 : 1226
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 50
REMARK 3 SOLVENT ATOMS : 194
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 23.20
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 30.90
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 2.67000
REMARK 3 B22 (A**2) : 2.67000
REMARK 3 B33 (A**2) : -5.34000
REMARK 3 B12 (A**2) : -0.32000
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) : 0.23
REMARK 3 ESD FROM SIGMAA (A) : 0.17
REMARK 3 LOW RESOLUTION CUTOFF (A) : 20.0
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) : 0.17
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.005
REMARK 3 BOND ANGLES (DEGREES) : 1.100
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 20.10
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.750
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) : 1.270 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 1.990 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 2.010 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 2.970 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.39
REMARK 3 BSOL : 53.77
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 : PARAM.ADP
REMARK 3 PARAMETER FILE 5 : PARAM.HEP
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 : ION.TOP
REMARK 3 TOPOLOGY FILE 4 : TOPOL.ADP
REMARK 3 TOPOLOGY FILE 5 : TOPOL.HEP
REMARK 3 TOPOLOGY FILE 6 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1L4U COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 07-MAR-02.
REMARK 100 THE DEPOSITION ID IS D_1000015646.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 03-AUG-99
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : NSLS
REMARK 200 BEAMLINE : X9B
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.07223,1.07186,1.06268,1.08121
REMARK 200 MONOCHROMATOR : SILICON (111) CHANNEL
REMARK 200 OPTICS : MIRROR
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 4
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 20594
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.800
REMARK 200 RESOLUTION RANGE LOW (A) : 19.020
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 200 DATA REDUNDANCY : 6.640
REMARK 200 R MERGE (I) : 0.10400
REMARK 200 R SYM (I) : 0.08000
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 10.1340
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) : 1.86
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.8
REMARK 200 DATA REDUNDANCY IN SHELL : 5.86
REMARK 200 R MERGE FOR SHELL (I) : 0.17600
REMARK 200 R SYM FOR SHELL (I) : 0.16500
REMARK 200 <I/SIGMA(I)> FOR SHELL : 4.340
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: MAD
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD
REMARK 200 SOFTWARE USED: PHASES
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 57.63
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.90
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 4000, MAGNESIUM CHOLORIDE, SODIUM
REMARK 280 CHLORIDE, ADENOSINE-5'-DIPHOSPHATE, SHIKIMIC ACID, NAHEPES,
REMARK 280 PLATINUM POTASSIUM CHLORIDE, PH 7.5, VAPOR DIFFUSION, HANGING
REMARK 280 DROP, TEMPERATURE 288K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32 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+2/3
REMARK 290 3555 -X+Y,-X,Z+1/3
REMARK 290 4555 Y,X,-Z
REMARK 290 5555 X-Y,-Y,-Z+1/3
REMARK 290 6555 -X,-X+Y,-Z+2/3
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 61.28000
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 30.64000
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 30.64000
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 61.28000
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: MONOMERIC
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 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 167
REMARK 465 VAL A 168
REMARK 465 PRO A 169
REMARK 465 SER A 170
REMARK 465 PRO A 171
REMARK 465 SER A 172
REMARK 465 GLU A 173
REMARK 465 ALA A 174
REMARK 465 ALA A 175
REMARK 465 THR A 176
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 THR A 115 CB OG1 CG2
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 OG SER A 16 O HOH A 394 2.11
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 51 -76.50 -67.82
REMARK 500 THR A 115 32.88 -78.00
REMARK 500 VAL A 116 82.08 72.01
REMARK 500 LEU A 120 57.12 -115.60
REMARK 500 ASP A 124 61.73 36.17
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 MG A 190 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 SER A 16 OG
REMARK 620 2 ADP A 180 O2B 74.0
REMARK 620 3 HOH A 296 O 62.4 70.1
REMARK 620 4 HOH A 350 O 113.1 119.1 169.3
REMARK 620 5 HOH A 374 O 134.7 98.9 73.1 109.2
REMARK 620 6 HOH A 393 O 80.0 146.8 79.8 89.9 84.9
REMARK 620 7 HOH A 394 O 43.0 96.0 104.4 70.2 162.7 77.9
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 PT A 189 PT
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 MET A 133 SD
REMARK 620 2 EPE A 181 N4 172.5
REMARK 620 3 EPE A 181 O8 109.2 71.0
REMARK 620 4 CL A 195 CL 65.4 121.3 76.6
REMARK 620 5 CL A 196 CL 83.9 91.5 141.8 139.2
REMARK 620 N 1 2 3 4
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PT A 189
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 190
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 191
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 192
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 193
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 194
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 195
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 196
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADP A 180
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EPE A 181
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1L4Y RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF SHIKIMATE KINASE FROM MYCOBACTERIUM
REMARK 900 TUBERCULOSIS IN COMPLEX WITH MGADP AT 2.0 ANGSTROM RESOLUTION
REMARK 900 RELATED ID: 1SHK RELATED DB: PDB
REMARK 900 THE THREE-DIMENSIONAL STRUCTURE OF SHIKIMATE KINASE FROM ERWINIA
REMARK 900 CHRYSANTHEMI
REMARK 900 RELATED ID: 2SHK RELATED DB: PDB
REMARK 900 THE THREE-DIMENSIONAL STRUCTURE OF SHIKIMATE KINASE FROM ERWINIA
REMARK 900 CHRYSANTHEMI COMPLEXED WITH ADP
REMARK 900 RELATED ID: 1E6C RELATED DB: PDB
REMARK 900 K15M MUTANT OF SHIKIMATE KINASE FROM ERWINIA CHRYSANTHEMI
DBREF 1L4U A 1 176 UNP P0A4Z2 AROK_MYCTU 1 176
SEQRES 1 A 176 MET ALA PRO LYS ALA VAL LEU VAL GLY LEU PRO GLY SER
SEQRES 2 A 176 GLY LYS SER THR ILE GLY ARG ARG LEU ALA LYS ALA LEU
SEQRES 3 A 176 GLY VAL GLY LEU LEU ASP THR ASP VAL ALA ILE GLU GLN
SEQRES 4 A 176 ARG THR GLY ARG SER ILE ALA ASP ILE PHE ALA THR ASP
SEQRES 5 A 176 GLY GLU GLN GLU PHE ARG ARG ILE GLU GLU ASP VAL VAL
SEQRES 6 A 176 ARG ALA ALA LEU ALA ASP HIS ASP GLY VAL LEU SER LEU
SEQRES 7 A 176 GLY GLY GLY ALA VAL THR SER PRO GLY VAL ARG ALA ALA
SEQRES 8 A 176 LEU ALA GLY HIS THR VAL VAL TYR LEU GLU ILE SER ALA
SEQRES 9 A 176 ALA GLU GLY VAL ARG ARG THR GLY GLY ASN THR VAL ARG
SEQRES 10 A 176 PRO LEU LEU ALA GLY PRO ASP ARG ALA GLU LYS TYR ARG
SEQRES 11 A 176 ALA LEU MET ALA LYS ARG ALA PRO LEU TYR ARG ARG VAL
SEQRES 12 A 176 ALA THR MET ARG VAL ASP THR ASN ARG ARG ASN PRO GLY
SEQRES 13 A 176 ALA VAL VAL ARG HIS ILE LEU SER ARG LEU GLN VAL PRO
SEQRES 14 A 176 SER PRO SER GLU ALA ALA THR
HET PT A 189 1
HET MG A 190 1
HET CL A 191 1
HET CL A 192 1
HET CL A 193 1
HET CL A 194 1
HET CL A 195 1
HET CL A 196 1
HET ADP A 180 27
HET EPE A 181 15
HETNAM PT PLATINUM (II) ION
HETNAM MG MAGNESIUM ION
HETNAM CL CHLORIDE ION
HETNAM ADP ADENOSINE-5'-DIPHOSPHATE
HETNAM EPE 4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID
HETSYN EPE HEPES
FORMUL 2 PT PT 2+
FORMUL 3 MG MG 2+
FORMUL 4 CL 6(CL 1-)
FORMUL 10 ADP C10 H15 N5 O10 P2
FORMUL 11 EPE C8 H18 N2 O4 S
FORMUL 12 HOH *194(H2 O)
HELIX 1 1 GLY A 14 GLY A 27 1 14
HELIX 2 2 THR A 33 GLY A 42 1 10
HELIX 3 3 SER A 44 ASP A 52 1 9
HELIX 4 4 GLY A 53 HIS A 72 1 20
HELIX 5 5 GLY A 81 THR A 84 5 4
HELIX 6 6 SER A 85 ALA A 93 1 9
HELIX 7 7 SER A 103 THR A 111 1 9
HELIX 8 8 ARG A 117 ALA A 121 5 5
HELIX 9 9 ASP A 124 ALA A 144 1 21
HELIX 10 10 ASN A 154 LEU A 166 1 13
SHEET 1 A 5 LEU A 30 ASP A 32 0
SHEET 2 A 5 VAL A 75 SER A 77 1 O VAL A 75 N LEU A 31
SHEET 3 A 5 ALA A 5 VAL A 8 1 N LEU A 7 O LEU A 76
SHEET 4 A 5 VAL A 97 GLU A 101 1 O VAL A 98 N VAL A 6
SHEET 5 A 5 MET A 146 ASP A 149 1 O MET A 146 N TYR A 99
LINK OG SER A 16 MG MG A 190 1555 1555 2.57
LINK SD MET A 133 PT PT A 189 1555 1555 2.46
LINK O2B ADP A 180 MG MG A 190 1555 1555 2.39
LINK N4 EPE A 181 PT PT A 189 1555 1555 2.41
LINK O8 EPE A 181 PT PT A 189 1555 1555 2.61
LINK PT PT A 189 CL CL A 195 1555 1555 2.24
LINK PT PT A 189 CL CL A 196 1555 1555 2.40
LINK MG MG A 190 O HOH A 296 1555 1555 2.94
LINK MG MG A 190 O HOH A 350 1555 1555 2.77
LINK MG MG A 190 O HOH A 374 1555 1555 2.52
LINK MG MG A 190 O HOH A 393 1555 1555 2.37
LINK MG MG A 190 O HOH A 394 1555 1555 3.06
SITE 1 AC1 4 MET A 133 EPE A 181 CL A 195 CL A 196
SITE 1 AC2 7 SER A 16 ADP A 180 HOH A 296 HOH A 350
SITE 2 AC2 7 HOH A 374 HOH A 393 HOH A 394
SITE 1 AC3 3 ARG A 66 ARG A 160 HOH A 204
SITE 1 AC4 4 GLY A 29 HIS A 72 GLY A 74 HOH A 235
SITE 1 AC5 4 PRO A 11 LYS A 15 GLY A 80 HOH A 367
SITE 1 AC6 4 LYS A 24 ARG A 66 ALA A 90 ARG A 109
SITE 1 AC7 4 MET A 133 EPE A 181 PT A 189 HOH A 321
SITE 1 AC8 4 ARG A 130 MET A 133 EPE A 181 PT A 189
SITE 1 AC9 18 LEU A 10 PRO A 11 GLY A 12 SER A 13
SITE 2 AC9 18 GLY A 14 LYS A 15 SER A 16 THR A 17
SITE 3 AC9 18 ARG A 110 ARG A 117 ARG A 153 PRO A 155
SITE 4 AC9 18 MG A 190 HOH A 213 HOH A 216 HOH A 256
SITE 5 AC9 18 HOH A 296 HOH A 356
SITE 1 BC1 10 THR A 96 ARG A 130 MET A 133 THR A 145
SITE 2 BC1 10 MET A 146 ARG A 165 PT A 189 CL A 195
SITE 3 BC1 10 CL A 196 HOH A 378
CRYST1 63.830 63.830 91.920 90.00 90.00 120.00 P 32 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 0.015666 0.009045 0.000000 0.00000
SCALE2 0.000000 0.018089 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010879 0.00000
(ATOM LINES ARE NOT SHOWN.)
END