HEADER TRANSFERASE 26-DEC-14 4RZX
TITLE CRYSTAL STRUCTURE (TYPE-3) OF DTMP KINASE (ST1543) FROM SULFOLOBUS
TITLE 2 TOKODAII STRAIN7
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROBABLE THYMIDYLATE KINASE;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: THYMIDYLATE KINASE;
COMPND 5 SYNONYM: DTMP KINASE;
COMPND 6 EC: 2.7.4.9;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SULFOLOBUS TOKODAII;
SOURCE 3 ORGANISM_TAXID: 273063;
SOURCE 4 STRAIN: STRAIN7;
SOURCE 5 GENE: STK_15430, TMK;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21-CODONPLUS (DE3)-RIL;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET21A
KEYWDS TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR A.BISWAS,J.JEYAKANTHAN,K.SEKAR
REVDAT 2 20-SEP-23 4RZX 1 REMARK LINK
REVDAT 1 30-DEC-15 4RZX 0
JRNL AUTH A.BISWAS,J.JEYAKANTHAN,K.SEKAR
JRNL TITL CRYSTAL STRUCTURE (TYPE-3) OF DTMP KINASE (ST1543) FROM
JRNL TITL 2 SULFOLOBUS TOKODAII STRAIN7
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.30 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0073
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.30
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.9
REMARK 3 NUMBER OF REFLECTIONS : 18955
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 + TEST SET) : 0.204
REMARK 3 R VALUE (WORKING SET) : 0.201
REMARK 3 FREE R VALUE : 0.259
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.200
REMARK 3 FREE R VALUE TEST SET COUNT : 1031
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) : 2.30
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.36
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1364
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 98.64
REMARK 3 BIN R VALUE (WORKING SET) : 0.2200
REMARK 3 BIN FREE R VALUE SET COUNT : 82
REMARK 3 BIN FREE R VALUE : 0.2550
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3137
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 11
REMARK 3 SOLVENT ATOMS : 16
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 59.45
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 3.06000
REMARK 3 B22 (A**2) : -0.92000
REMARK 3 B33 (A**2) : -2.14000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.336
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.249
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.191
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 9.800
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.954
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.930
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 3222 ; 0.015 ; 0.020
REMARK 3 BOND LENGTHS OTHERS (A): 3010 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 4384 ; 1.695 ; 1.967
REMARK 3 BOND ANGLES OTHERS (DEGREES): 6887 ; 0.855 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 403 ; 6.081 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 131 ;32.958 ;23.359
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 511 ;15.593 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 18 ;20.815 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 507 ; 0.087 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 3584 ; 0.008 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 718 ; 0.001 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 1621 ; 3.760 ; 4.506
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 1620 ; 3.759 ; 4.505
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2018 ; 5.305 ; 6.734
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 2019 ; 5.353 ; 7.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1601 ; 4.069 ; 4.730
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 1612 ; 4.222 ; 4.930
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 2376 ; 6.125 ; 7.241
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 3830 ; 8.099 ;37.576
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 3829 ; 8.100 ;37.570
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 2
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 31 A 59
REMARK 3 RESIDUE RANGE : A 144 A 183
REMARK 3 ORIGIN FOR THE GROUP (A): -33.289 -1.195 24.018
REMARK 3 T TENSOR
REMARK 3 T11: 0.3136 T22: 0.1728
REMARK 3 T33: 0.2388 T12: 0.0401
REMARK 3 T13: -0.0113 T23: -0.0496
REMARK 3 L TENSOR
REMARK 3 L11: 1.4419 L22: 2.8368
REMARK 3 L33: 0.6116 L12: 1.2004
REMARK 3 L13: -0.8570 L23: -1.1427
REMARK 3 S TENSOR
REMARK 3 S11: 0.1343 S12: -0.1448 S13: 0.1103
REMARK 3 S21: 0.3796 S22: -0.0680 S23: 0.0875
REMARK 3 S31: -0.1605 S32: 0.0601 S33: -0.0663
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 5
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 32 B 43
REMARK 3 RESIDUE RANGE : B 44 B 77
REMARK 3 RESIDUE RANGE : B 78 B 94
REMARK 3 RESIDUE RANGE : B 95 B 183
REMARK 3 RESIDUE RANGE : B 184 B 208
REMARK 3 ORIGIN FOR THE GROUP (A): -12.285 1.242 -2.039
REMARK 3 T TENSOR
REMARK 3 T11: 0.2077 T22: 0.0611
REMARK 3 T33: 0.1392 T12: -0.0567
REMARK 3 T13: 0.0203 T23: -0.0254
REMARK 3 L TENSOR
REMARK 3 L11: 2.5084 L22: 1.7628
REMARK 3 L33: 2.2192 L12: -0.1483
REMARK 3 L13: -1.2566 L23: 0.0889
REMARK 3 S TENSOR
REMARK 3 S11: -0.1543 S12: -0.0769 S13: 0.0412
REMARK 3 S21: -0.0516 S22: 0.1033 S23: -0.1842
REMARK 3 S31: 0.2092 S32: -0.0288 S33: 0.0510
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 4RZX COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 05-JAN-15.
REMARK 100 THE DEPOSITION ID IS D_1000088004.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SPRING-8
REMARK 200 BEAMLINE : BL26B2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9000
REMARK 200 MONOCHROMATOR : SI-1 1 1 DOUBLE CRYSTAL
REMARK 200 MONOCHROMATOR
REMARK 200 OPTICS : RH COATED BENT-CYRINDRICAL
REMARK 200 MIRROR
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS V
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 20021
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.300
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.0
REMARK 200 DATA REDUNDANCY : 7.200
REMARK 200 R MERGE (I) : 0.09000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 19.3480
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.30
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.34
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 7.40
REMARK 200 R MERGE FOR SHELL (I) : 0.39500
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 4.660
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: 2PLR
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 44.59
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.22
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.01 M MAGNESIUM CHLORIDE HEXAHYDRATE,
REMARK 280 0.005 M NICKEL(II) CHLORIDE HEXAHYDRATE, 0.1 M HEPES SODIUM, 15%
REMARK 280 W/V POLYETHYLENE GLYCOL 3,350, 0.5 M SODIUM FLUORIDE, PH 7.0,
REMARK 280 MICROBATCH UNDEROIL, TEMPERATURE 293.0K, EVAPORATION
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 24.96700
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 69.28250
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 31.61100
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 69.28250
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 24.96700
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 31.61100
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: 2660 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 18300 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -36.0 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 LYS A 2
REMARK 465 LYS A 143
REMARK 465 ASN A 211
REMARK 465 SER A 212
REMARK 465 PHE A 213
REMARK 465 MET B 1
REMARK 465 LYS B 2
REMARK 465 TRP B 39
REMARK 465 ASN B 40
REMARK 465 SER B 41
REMARK 465 SER B 42
REMARK 465 LYS B 54
REMARK 465 LYS B 55
REMARK 465 ASP B 56
REMARK 465 ILE B 209
REMARK 465 ASP B 210
REMARK 465 ASN B 211
REMARK 465 SER B 212
REMARK 465 PHE B 213
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 LYS A 3 CG CD CE NZ
REMARK 470 LYS A 25 NZ
REMARK 470 LYS A 31 CD CE NZ
REMARK 470 SER A 41 OG
REMARK 470 LYS A 54 CG CD CE NZ
REMARK 470 LYS A 55 CG CD CE NZ
REMARK 470 GLU A 76 CG CD OE1 OE2
REMARK 470 LYS A 84 CG CD CE NZ
REMARK 470 TYR A 96 CE2
REMARK 470 ASP A 110 CG OD1 OD2
REMARK 470 LYS A 113 CE NZ
REMARK 470 LYS A 121 CE NZ
REMARK 470 GLU A 137 CG CD OE1 OE2
REMARK 470 LYS A 141 CG CD CE NZ
REMARK 470 ARG A 144 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 145 CE NZ
REMARK 470 LYS A 147 CD CE NZ
REMARK 470 GLN A 149 CG CD OE1 NE2
REMARK 470 GLU A 163 CG CD OE1 OE2
REMARK 470 LYS A 167 CE NZ
REMARK 470 LYS A 178 CE NZ
REMARK 470 LYS A 181 CG CD CE NZ
REMARK 470 LYS A 195 CG CD CE NZ
REMARK 470 GLU A 196 CG CD OE1 OE2
REMARK 470 LYS A 203 CG CD CE NZ
REMARK 470 GLU A 207 CG CD OE1 OE2
REMARK 470 LYS B 25 CG CD CE NZ
REMARK 470 GLU B 38 CG CD OE1 OE2
REMARK 470 HIS B 46 CG ND1 CD2 CE1 NE2
REMARK 470 ASP B 47 CG OD1 OD2
REMARK 470 ILE B 49 CG1 CG2 CD1
REMARK 470 LYS B 50 CG CD CE NZ
REMARK 470 LYS B 53 CG CD CE NZ
REMARK 470 LEU B 57 CG CD1 CD2
REMARK 470 ARG B 93 CG CD NE CZ NH1 NH2
REMARK 470 LYS B 114 CG CD CE NZ
REMARK 470 GLU B 137 CG CD OE1 OE2
REMARK 470 LYS B 140 CE NZ
REMARK 470 LYS B 141 CG CD CE NZ
REMARK 470 LYS B 143 CG CD CE NZ
REMARK 470 LYS B 145 CG CD CE NZ
REMARK 470 GLN B 149 CG CD OE1 NE2
REMARK 470 LEU B 159 CG CD1 CD2
REMARK 470 GLU B 162 CG CD OE1 OE2
REMARK 470 LYS B 167 CD CE NZ
REMARK 470 LYS B 181 CG CD CE NZ
REMARK 470 ILE B 199 CG1 CG2 CD1
REMARK 470 LYS B 203 CG CD CE NZ
REMARK 470 GLU B 207 CG CD OE1 OE2
REMARK 470 LEU B 208 CG CD1 CD2
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 43 -157.28 -115.51
REMARK 500 SER A 85 14.51 -65.01
REMARK 500 ARG A 93 135.40 73.29
REMARK 500 TYR A 94 -158.93 -138.16
REMARK 500 SER A 160 138.50 -39.20
REMARK 500 LEU A 208 -71.51 -63.30
REMARK 500 ARG B 32 -178.04 178.62
REMARK 500 TYR B 94 -151.18 -147.71
REMARK 500 ASP B 108 102.80 -42.44
REMARK 500 GLU B 207 -72.80 -64.15
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 NI A 302 NI
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 46 NE2
REMARK 620 2 LYS A 50 NZ 98.9
REMARK 620 3 HIS A 67 NE2 105.1 105.7
REMARK 620 4 HOH A 409 O 164.2 76.8 90.7
REMARK 620 5 HOH A 410 O 90.1 163.9 84.7 91.0
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 PO4 A 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NI A 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 B 301
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2PLR RELATED DB: PDB
REMARK 900 RELATED ID: 4NZY RELATED DB: PDB
DBREF 4RZX A 1 213 UNP Q970Q8 KTHY2_SULTO 1 213
DBREF 4RZX B 1 213 UNP Q970Q8 KTHY2_SULTO 1 213
SEQRES 1 A 213 MET LYS LYS GLY VAL LEU ILE ALA PHE GLU GLY ILE ASP
SEQRES 2 A 213 GLY SER GLY LYS SER SER GLN ALA THR LEU LEU LYS ASP
SEQRES 3 A 213 TRP ILE GLU LEU LYS ARG ASP VAL TYR LEU THR GLU TRP
SEQRES 4 A 213 ASN SER SER ASP TRP ILE HIS ASP ILE ILE LYS GLU ALA
SEQRES 5 A 213 LYS LYS LYS ASP LEU LEU THR PRO LEU THR PHE SER LEU
SEQRES 6 A 213 ILE HIS ALA THR ASP PHE SER ASP ARG TYR GLU ARG TYR
SEQRES 7 A 213 ILE LEU PRO MET LEU LYS SER GLY PHE ILE VAL ILE SER
SEQRES 8 A 213 ASP ARG TYR ILE TYR THR ALA TYR ALA ARG ASP SER VAL
SEQRES 9 A 213 ARG GLY VAL ASP ILE ASP TRP VAL LYS LYS LEU TYR SER
SEQRES 10 A 213 PHE ALA ILE LYS PRO ASP ILE THR PHE TYR ILE ARG VAL
SEQRES 11 A 213 SER PRO ASP ILE ALA LEU GLU ARG ILE LYS LYS SER LYS
SEQRES 12 A 213 ARG LYS ILE LYS PRO GLN GLU ALA GLY ALA ASP ILE PHE
SEQRES 13 A 213 PRO GLY LEU SER PRO GLU GLU GLY PHE LEU LYS TYR GLN
SEQRES 14 A 213 GLY LEU ILE THR GLU VAL TYR ASP LYS LEU VAL LYS ASP
SEQRES 15 A 213 GLU ASN PHE ILE VAL ILE ASP GLY THR LYS THR PRO LYS
SEQRES 16 A 213 GLU ILE GLN ILE GLN ILE ARG LYS PHE VAL GLY GLU LEU
SEQRES 17 A 213 ILE ASP ASN SER PHE
SEQRES 1 B 213 MET LYS LYS GLY VAL LEU ILE ALA PHE GLU GLY ILE ASP
SEQRES 2 B 213 GLY SER GLY LYS SER SER GLN ALA THR LEU LEU LYS ASP
SEQRES 3 B 213 TRP ILE GLU LEU LYS ARG ASP VAL TYR LEU THR GLU TRP
SEQRES 4 B 213 ASN SER SER ASP TRP ILE HIS ASP ILE ILE LYS GLU ALA
SEQRES 5 B 213 LYS LYS LYS ASP LEU LEU THR PRO LEU THR PHE SER LEU
SEQRES 6 B 213 ILE HIS ALA THR ASP PHE SER ASP ARG TYR GLU ARG TYR
SEQRES 7 B 213 ILE LEU PRO MET LEU LYS SER GLY PHE ILE VAL ILE SER
SEQRES 8 B 213 ASP ARG TYR ILE TYR THR ALA TYR ALA ARG ASP SER VAL
SEQRES 9 B 213 ARG GLY VAL ASP ILE ASP TRP VAL LYS LYS LEU TYR SER
SEQRES 10 B 213 PHE ALA ILE LYS PRO ASP ILE THR PHE TYR ILE ARG VAL
SEQRES 11 B 213 SER PRO ASP ILE ALA LEU GLU ARG ILE LYS LYS SER LYS
SEQRES 12 B 213 ARG LYS ILE LYS PRO GLN GLU ALA GLY ALA ASP ILE PHE
SEQRES 13 B 213 PRO GLY LEU SER PRO GLU GLU GLY PHE LEU LYS TYR GLN
SEQRES 14 B 213 GLY LEU ILE THR GLU VAL TYR ASP LYS LEU VAL LYS ASP
SEQRES 15 B 213 GLU ASN PHE ILE VAL ILE ASP GLY THR LYS THR PRO LYS
SEQRES 16 B 213 GLU ILE GLN ILE GLN ILE ARG LYS PHE VAL GLY GLU LEU
SEQRES 17 B 213 ILE ASP ASN SER PHE
HET PO4 A 301 5
HET NI A 302 1
HET PO4 B 301 5
HETNAM PO4 PHOSPHATE ION
HETNAM NI NICKEL (II) ION
FORMUL 3 PO4 2(O4 P 3-)
FORMUL 4 NI NI 2+
FORMUL 6 HOH *16(H2 O)
HELIX 1 1 GLY A 16 ARG A 32 1 17
HELIX 2 2 ASP A 43 LYS A 53 1 11
HELIX 3 3 THR A 59 TYR A 78 1 20
HELIX 4 4 TYR A 78 SER A 85 1 8
HELIX 5 5 TYR A 94 VAL A 104 1 11
HELIX 6 6 ASP A 108 TYR A 116 1 9
HELIX 7 7 SER A 131 SER A 142 1 12
HELIX 8 8 SER A 160 ASN A 184 1 25
HELIX 9 9 THR A 193 ASP A 210 1 18
HELIX 10 10 GLY B 16 GLU B 29 1 14
HELIX 11 11 TRP B 44 ALA B 52 1 9
HELIX 12 12 THR B 59 TYR B 78 1 20
HELIX 13 13 TYR B 78 SER B 85 1 8
HELIX 14 14 TYR B 94 VAL B 104 1 11
HELIX 15 15 ASP B 108 TYR B 116 1 9
HELIX 16 16 SER B 131 SER B 142 1 12
HELIX 17 17 LYS B 147 GLY B 152 1 6
HELIX 18 18 SER B 160 ASN B 184 1 25
HELIX 19 19 THR B 193 LEU B 208 1 16
SHEET 1 A 5 VAL A 34 GLU A 38 0
SHEET 2 A 5 ILE A 88 ASP A 92 1 O ILE A 88 N TYR A 35
SHEET 3 A 5 VAL A 5 GLU A 10 1 N ILE A 7 O VAL A 89
SHEET 4 A 5 ILE A 124 ARG A 129 1 O PHE A 126 N GLU A 10
SHEET 5 A 5 ILE A 186 ASP A 189 1 O ILE A 186 N THR A 125
SHEET 1 B 5 VAL B 34 LEU B 36 0
SHEET 2 B 5 ILE B 88 SER B 91 1 O ILE B 90 N TYR B 35
SHEET 3 B 5 VAL B 5 GLU B 10 1 N ILE B 7 O VAL B 89
SHEET 4 B 5 ILE B 124 ARG B 129 1 O PHE B 126 N GLU B 10
SHEET 5 B 5 PHE B 185 ASP B 189 1 O ILE B 188 N TYR B 127
LINK NE2 HIS A 46 NI NI A 302 1555 1555 2.23
LINK NZ LYS A 50 NI NI A 302 1555 1555 2.10
LINK NE2 HIS A 67 NI NI A 302 1555 1555 2.09
LINK NI NI A 302 O HOH A 409 1555 1555 2.26
LINK NI NI A 302 O HOH A 410 1555 1555 1.81
SITE 1 AC1 7 ILE A 12 ASP A 13 GLY A 14 SER A 15
SITE 2 AC1 7 GLY A 16 LYS A 17 SER A 18
SITE 1 AC2 5 HIS A 46 LYS A 50 HIS A 67 HOH A 409
SITE 2 AC2 5 HOH A 410
SITE 1 AC3 6 ILE B 12 GLY B 14 SER B 15 GLY B 16
SITE 2 AC3 6 LYS B 17 SER B 18
CRYST1 49.934 63.222 138.565 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 0.020026 0.000000 0.000000 0.00000
SCALE2 0.000000 0.015817 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007217 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
