HEADER TRANSFERASE 18-MAR-09 3GO6
TITLE CRYSTAL STRUCTURE OF M. TUBERCULOSIS RIBOKINASE (RV2436) IN COMPLEX
TITLE 2 WITH RIBOSE AND AMP-PNP
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: RIBOKINASE RBSK;
COMPND 3 CHAIN: A, B;
COMPND 4 EC: 2.7.1.15;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MYCOBACTERIUM TUBERCULOSIS;
SOURCE 3 ORGANISM_TAXID: 1773;
SOURCE 4 STRAIN: H37RV;
SOURCE 5 GENE: RBSK, RV2436;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET28
KEYWDS PHOSPHOFRUCTOKINASE, CARBOHYDRATE KINASE, KINASE, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR E.I.MASTERS,Y.SUN,Y.WANG,W.B.PARKER,R.LI
REVDAT 5 21-FEB-24 3GO6 1 HETSYN
REVDAT 4 29-JUL-20 3GO6 1 COMPND REMARK SEQADV HETNAM
REVDAT 4 2 1 LINK SITE ATOM
REVDAT 3 24-JAN-18 3GO6 1 JRNL
REVDAT 2 01-NOV-17 3GO6 1 REMARK
REVDAT 1 31-MAR-10 3GO6 0
JRNL AUTH E.I.MASTERS,Y.SUN,Y.WANG,W.B.PARKER,R.LI
JRNL TITL CRYSTAL STRUCTURE AND BIOCHEMICAL CHARACTERIZATION OF
JRNL TITL 2 M.TUBERCULOSIS RIBOKINASE (RV2436)
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.98 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC
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) : 1.98
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 48.17
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 3 NUMBER OF REFLECTIONS : 52460
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) : 0.172
REMARK 3 R VALUE (WORKING SET) : 0.170
REMARK 3 FREE R VALUE : 0.203
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 2674
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) : 1.98
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.03
REMARK 3 REFLECTION IN BIN (WORKING SET) : 3587
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 98.07
REMARK 3 BIN R VALUE (WORKING SET) : 0.1940
REMARK 3 BIN FREE R VALUE SET COUNT : 217
REMARK 3 BIN FREE R VALUE : 0.2410
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4010
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 39
REMARK 3 SOLVENT ATOMS : 507
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 25.25
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.27000
REMARK 3 B22 (A**2) : 0.41000
REMARK 3 B33 (A**2) : 0.51000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.80000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.131
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.124
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.080
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.768
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.958
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.934
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 4121 ; 0.012 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 5677 ; 1.300 ; 1.969
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 572 ; 5.681 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 148 ;35.606 ;23.649
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 522 ;11.649 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 34 ;16.434 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 698 ; 0.084 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 3185 ; 0.004 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 1906 ; 0.194 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 2874 ; 0.295 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 390 ; 0.134 ; 0.200
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): 78 ; 0.188 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 20 ; 0.141 ; 0.200
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): 2917 ; 0.855 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 4564 ; 1.450 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1314 ; 2.173 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1113 ; 3.690 ; 4.500
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
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 : NULL
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 3GO6 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 31-MAR-09.
REMARK 100 THE DEPOSITION ID IS D_1000052105.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 30-JUL-08
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 22-BM
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.00
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : ROSENBAUM-ROCK MONOCHROMATOR
REMARK 200 HIGH-RESOLUTION DOUBLE-CRYSTAL
REMARK 200 SI (111) SAGITTAL FOCUSING.
REMARK 200 ROSENBAUM-ROCK VERTICAL FOCUSING
REMARK 200 MIRROR.
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 225 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO, HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK, HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 52512
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.980
REMARK 200 RESOLUTION RANGE LOW (A) : 48.170
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 200 DATA REDUNDANCY : 3.800
REMARK 200 R MERGE (I) : 0.03900
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 29.1460
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.98
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.05
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 3.80
REMARK 200 R MERGE FOR SHELL (I) : 0.13900
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: PHASER
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 60.41
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.11
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M SODIUM/POTASSIUM PHOSPHATE, 0.1
REMARK 280 M BIS-TRIS PROPANE, 16% PEG 3350, PH 6.5, VAPOR DIFFUSION,
REMARK 280 TEMPERATURE 295K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y,-Z
REMARK 290 3555 X+1/2,Y+1/2,Z
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 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 39.21200
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 58.95000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 39.21200
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 58.95000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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: 3750 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 21730 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -26.0 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 APPLY THE FOLLOWING TO CHAINS: B
REMARK 350 BIOMT1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 9470 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 41490 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -62.0 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 -1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 0.000000 1.000000 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 -5
REMARK 465 HIS A -4
REMARK 465 HIS A -3
REMARK 465 HIS A -2
REMARK 465 HIS A -1
REMARK 465 HIS A 0
REMARK 465 HIS A 1
REMARK 465 ALA A 2
REMARK 465 ASN A 3
REMARK 465 ALA A 4
REMARK 465 SER A 5
REMARK 465 GLU A 6
REMARK 465 THR A 7
REMARK 465 ASN A 8
REMARK 465 VAL A 9
REMARK 465 GLY A 10
REMARK 465 PRO A 11
REMARK 465 MET A 12
REMARK 465 ARG A 300
REMARK 465 HIS A 301
REMARK 465 ASN A 302
REMARK 465 GLY A 303
REMARK 465 SER A 304
REMARK 465 MET B -5
REMARK 465 HIS B -4
REMARK 465 HIS B -3
REMARK 465 HIS B -2
REMARK 465 HIS B -1
REMARK 465 HIS B 0
REMARK 465 HIS B 1
REMARK 465 ALA B 2
REMARK 465 ASN B 3
REMARK 465 ALA B 4
REMARK 465 SER B 5
REMARK 465 GLU B 6
REMARK 465 THR B 7
REMARK 465 ASN B 8
REMARK 465 VAL B 9
REMARK 465 GLY B 10
REMARK 465 PRO B 11
REMARK 465 MET B 12
REMARK 465 ARG B 300
REMARK 465 HIS B 301
REMARK 465 ASN B 302
REMARK 465 GLY B 303
REMARK 465 SER B 304
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 75 48.55 -101.43
REMARK 500 ASP A 176 105.42 -56.28
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 306 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 236 O
REMARK 620 2 ALA A 238 O 87.5
REMARK 620 3 ALA A 276 O 85.1 123.0
REMARK 620 4 VAL A 279 O 87.3 152.7 83.1
REMARK 620 5 GLY A 281 O 136.5 82.3 135.1 83.3
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG B 306 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 236 O
REMARK 620 2 ALA B 238 O 88.4
REMARK 620 3 ALA B 276 O 79.9 118.7
REMARK 620 4 VAL B 279 O 85.7 156.2 83.0
REMARK 620 5 GLY B 281 O 141.4 82.0 137.0 88.3
REMARK 620 N 1 2 3 4
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3GO7 RELATED DB: PDB
REMARK 900 THE SAME PROTEIN WITH RIBOSE ONLY.
REMARK 900 RELATED ID: 1RKD RELATED DB: PDB
REMARK 900 RIBOKINASE STRUCTURE FROM E.COLI.
REMARK 900 RELATED ID: 2FV7 RELATED DB: PDB
REMARK 900 RIBOKINASE STRUCTURE FROM HUMAN.
DBREF 3GO6 A 2 304 UNP P71913 P71913_MYCTU 2 304
DBREF 3GO6 B 2 304 UNP P71913 P71913_MYCTU 2 304
SEQADV 3GO6 MET A -5 UNP P71913 EXPRESSION TAG
SEQADV 3GO6 HIS A -4 UNP P71913 EXPRESSION TAG
SEQADV 3GO6 HIS A -3 UNP P71913 EXPRESSION TAG
SEQADV 3GO6 HIS A -2 UNP P71913 EXPRESSION TAG
SEQADV 3GO6 HIS A -1 UNP P71913 EXPRESSION TAG
SEQADV 3GO6 HIS A 0 UNP P71913 EXPRESSION TAG
SEQADV 3GO6 HIS A 1 UNP P71913 EXPRESSION TAG
SEQADV 3GO6 MET B -5 UNP P71913 EXPRESSION TAG
SEQADV 3GO6 HIS B -4 UNP P71913 EXPRESSION TAG
SEQADV 3GO6 HIS B -3 UNP P71913 EXPRESSION TAG
SEQADV 3GO6 HIS B -2 UNP P71913 EXPRESSION TAG
SEQADV 3GO6 HIS B -1 UNP P71913 EXPRESSION TAG
SEQADV 3GO6 HIS B 0 UNP P71913 EXPRESSION TAG
SEQADV 3GO6 HIS B 1 UNP P71913 EXPRESSION TAG
SEQRES 1 A 310 MET HIS HIS HIS HIS HIS HIS ALA ASN ALA SER GLU THR
SEQRES 2 A 310 ASN VAL GLY PRO MET ALA PRO ARG VAL CYS VAL VAL GLY
SEQRES 3 A 310 SER VAL ASN MET ASP LEU THR PHE VAL VAL ASP ALA LEU
SEQRES 4 A 310 PRO ARG PRO GLY GLU THR VAL LEU ALA ALA SER LEU THR
SEQRES 5 A 310 ARG THR PRO GLY GLY LYS GLY ALA ASN GLN ALA VAL ALA
SEQRES 6 A 310 ALA ALA ARG ALA GLY ALA GLN VAL GLN PHE SER GLY ALA
SEQRES 7 A 310 PHE GLY ASP ASP PRO ALA ALA ALA GLN LEU ARG ALA HIS
SEQRES 8 A 310 LEU ARG ALA ASN ALA VAL GLY LEU ASP ARG THR VAL THR
SEQRES 9 A 310 VAL PRO GLY PRO SER GLY THR ALA ILE ILE VAL VAL ASP
SEQRES 10 A 310 ALA SER ALA GLU ASN THR VAL LEU VAL ALA PRO GLY ALA
SEQRES 11 A 310 ASN ALA HIS LEU THR PRO VAL PRO SER ALA VAL ALA ASN
SEQRES 12 A 310 CYS ASP VAL LEU LEU THR GLN LEU GLU ILE PRO VAL ALA
SEQRES 13 A 310 THR ALA LEU ALA ALA ALA ARG ALA ALA GLN SER ALA ASP
SEQRES 14 A 310 ALA VAL VAL MET VAL ASN ALA SER PRO ALA GLY GLN ASP
SEQRES 15 A 310 ARG SER SER LEU GLN ASP LEU ALA ALA ILE ALA ASP VAL
SEQRES 16 A 310 VAL ILE ALA ASN GLU HIS GLU ALA ASN ASP TRP PRO SER
SEQRES 17 A 310 PRO PRO THR HIS PHE VAL ILE THR LEU GLY VAL ARG GLY
SEQRES 18 A 310 ALA ARG TYR VAL GLY ALA ASP GLY VAL PHE GLU VAL PRO
SEQRES 19 A 310 ALA PRO THR VAL THR PRO VAL ASP THR ALA GLY ALA GLY
SEQRES 20 A 310 ASP VAL PHE ALA GLY VAL LEU ALA ALA ASN TRP PRO ARG
SEQRES 21 A 310 ASN PRO GLY SER PRO ALA GLU ARG LEU ARG ALA LEU ARG
SEQRES 22 A 310 ARG ALA CYS ALA ALA GLY ALA LEU ALA THR LEU VAL SER
SEQRES 23 A 310 GLY VAL GLY ASP CYS ALA PRO ALA ALA ALA ALA ILE ASP
SEQRES 24 A 310 ALA ALA LEU ARG ALA ASN ARG HIS ASN GLY SER
SEQRES 1 B 310 MET HIS HIS HIS HIS HIS HIS ALA ASN ALA SER GLU THR
SEQRES 2 B 310 ASN VAL GLY PRO MET ALA PRO ARG VAL CYS VAL VAL GLY
SEQRES 3 B 310 SER VAL ASN MET ASP LEU THR PHE VAL VAL ASP ALA LEU
SEQRES 4 B 310 PRO ARG PRO GLY GLU THR VAL LEU ALA ALA SER LEU THR
SEQRES 5 B 310 ARG THR PRO GLY GLY LYS GLY ALA ASN GLN ALA VAL ALA
SEQRES 6 B 310 ALA ALA ARG ALA GLY ALA GLN VAL GLN PHE SER GLY ALA
SEQRES 7 B 310 PHE GLY ASP ASP PRO ALA ALA ALA GLN LEU ARG ALA HIS
SEQRES 8 B 310 LEU ARG ALA ASN ALA VAL GLY LEU ASP ARG THR VAL THR
SEQRES 9 B 310 VAL PRO GLY PRO SER GLY THR ALA ILE ILE VAL VAL ASP
SEQRES 10 B 310 ALA SER ALA GLU ASN THR VAL LEU VAL ALA PRO GLY ALA
SEQRES 11 B 310 ASN ALA HIS LEU THR PRO VAL PRO SER ALA VAL ALA ASN
SEQRES 12 B 310 CYS ASP VAL LEU LEU THR GLN LEU GLU ILE PRO VAL ALA
SEQRES 13 B 310 THR ALA LEU ALA ALA ALA ARG ALA ALA GLN SER ALA ASP
SEQRES 14 B 310 ALA VAL VAL MET VAL ASN ALA SER PRO ALA GLY GLN ASP
SEQRES 15 B 310 ARG SER SER LEU GLN ASP LEU ALA ALA ILE ALA ASP VAL
SEQRES 16 B 310 VAL ILE ALA ASN GLU HIS GLU ALA ASN ASP TRP PRO SER
SEQRES 17 B 310 PRO PRO THR HIS PHE VAL ILE THR LEU GLY VAL ARG GLY
SEQRES 18 B 310 ALA ARG TYR VAL GLY ALA ASP GLY VAL PHE GLU VAL PRO
SEQRES 19 B 310 ALA PRO THR VAL THR PRO VAL ASP THR ALA GLY ALA GLY
SEQRES 20 B 310 ASP VAL PHE ALA GLY VAL LEU ALA ALA ASN TRP PRO ARG
SEQRES 21 B 310 ASN PRO GLY SER PRO ALA GLU ARG LEU ARG ALA LEU ARG
SEQRES 22 B 310 ARG ALA CYS ALA ALA GLY ALA LEU ALA THR LEU VAL SER
SEQRES 23 B 310 GLY VAL GLY ASP CYS ALA PRO ALA ALA ALA ALA ILE ASP
SEQRES 24 B 310 ALA ALA LEU ARG ALA ASN ARG HIS ASN GLY SER
HET RIB A 305 10
HET MG A 306 1
HET ADP B 305 27
HET MG B 306 1
HETNAM RIB ALPHA-D-RIBOFURANOSE
HETNAM MG MAGNESIUM ION
HETNAM ADP ADENOSINE-5'-DIPHOSPHATE
HETSYN RIB ALPHA-D-RIBOSE; D-RIBOSE; RIBOSE
FORMUL 3 RIB C5 H10 O5
FORMUL 4 MG 2(MG 2+)
FORMUL 5 ADP C10 H15 N5 O10 P2
FORMUL 7 HOH *507(H2 O)
HELIX 1 1 GLY A 51 ALA A 63 1 13
HELIX 2 2 ASP A 76 ASN A 89 1 14
HELIX 3 3 PRO A 122 LEU A 128 5 7
HELIX 4 4 PRO A 148 ALA A 162 1 15
HELIX 5 5 ASP A 176 ALA A 187 1 12
HELIX 6 6 GLU A 194 TRP A 200 1 7
HELIX 7 7 GLY A 212 ARG A 214 5 3
HELIX 8 8 GLY A 239 TRP A 252 1 14
HELIX 9 9 SER A 258 THR A 277 1 20
HELIX 10 10 ALA A 288 ALA A 298 1 11
HELIX 11 11 GLY B 51 ALA B 63 1 13
HELIX 12 12 ASP B 76 ASN B 89 1 14
HELIX 13 13 PRO B 122 LEU B 128 5 7
HELIX 14 14 VAL B 131 ALA B 136 5 6
HELIX 15 15 PRO B 148 ALA B 162 1 15
HELIX 16 16 ARG B 177 SER B 179 5 3
HELIX 17 17 LEU B 180 ALA B 187 1 8
HELIX 18 18 GLU B 194 ASP B 199 1 6
HELIX 19 19 GLY B 212 ARG B 214 5 3
HELIX 20 20 GLY B 239 TRP B 252 1 14
HELIX 21 21 SER B 258 THR B 277 1 20
HELIX 22 22 ALA B 288 ALA B 298 1 11
SHEET 1 A 8 GLN A 66 SER A 70 0
SHEET 2 A 8 ARG A 15 VAL A 19 1 N VAL A 18 O GLN A 68
SHEET 3 A 8 VAL A 140 THR A 143 1 O LEU A 142 N CYS A 17
SHEET 4 A 8 VAL A 165 ASN A 169 1 O ASN A 169 N THR A 143
SHEET 5 A 8 VAL A 189 ASN A 193 1 O ILE A 191 N VAL A 168
SHEET 6 A 8 HIS A 206 THR A 210 1 O VAL A 208 N VAL A 190
SHEET 7 A 8 ALA A 216 GLY A 220 -1 O ARG A 217 N ILE A 209
SHEET 8 A 8 GLY A 223 VAL A 227 -1 O PHE A 225 N TYR A 218
SHEET 1 B 4 SER A 44 GLY A 50 0
SHEET 2 B 4 ASN A 23 VAL A 29 -1 N ASP A 25 O THR A 48
SHEET 3 B 4 GLY A 104 VAL A 110 1 O ILE A 108 N PHE A 28
SHEET 4 B 4 ASN A 116 ALA A 121 -1 O LEU A 119 N ILE A 107
SHEET 1 C 2 ALA A 72 PHE A 73 0
SHEET 2 C 2 VAL A 97 THR A 98 1 O VAL A 97 N PHE A 73
SHEET 1 D 8 GLN B 66 SER B 70 0
SHEET 2 D 8 ARG B 15 VAL B 19 1 N VAL B 18 O GLN B 68
SHEET 3 D 8 VAL B 140 GLN B 144 1 O LEU B 142 N CYS B 17
SHEET 4 D 8 VAL B 165 ASN B 169 1 O VAL B 165 N LEU B 141
SHEET 5 D 8 VAL B 189 ASN B 193 1 O VAL B 189 N VAL B 168
SHEET 6 D 8 HIS B 206 THR B 210 1 O VAL B 208 N VAL B 190
SHEET 7 D 8 ALA B 216 GLY B 220 -1 O ARG B 217 N ILE B 209
SHEET 8 D 8 GLY B 223 VAL B 227 -1 O VAL B 227 N ALA B 216
SHEET 1 E 4 SER B 44 GLY B 50 0
SHEET 2 E 4 ASN B 23 VAL B 29 -1 N ASP B 25 O THR B 48
SHEET 3 E 4 GLY B 104 VAL B 110 1 O ALA B 106 N LEU B 26
SHEET 4 E 4 ASN B 116 ALA B 121 -1 O LEU B 119 N ILE B 107
SHEET 1 F 2 ALA B 72 PHE B 73 0
SHEET 2 F 2 VAL B 97 THR B 98 1 O VAL B 97 N PHE B 73
LINK O ASP A 236 MG MG A 306 1555 1555 2.77
LINK O ALA A 238 MG MG A 306 1555 1555 2.78
LINK O ALA A 276 MG MG A 306 1555 1555 2.82
LINK O VAL A 279 MG MG A 306 1555 1555 2.67
LINK O GLY A 281 MG MG A 306 1555 1555 2.76
LINK O ASP B 236 MG MG B 306 1555 1555 2.79
LINK O ALA B 238 MG MG B 306 1555 1555 2.62
LINK O ALA B 276 MG MG B 306 1555 1555 2.78
LINK O VAL B 279 MG MG B 306 1555 1555 2.55
LINK O GLY B 281 MG MG B 306 1555 1555 2.79
CISPEP 1 SER A 171 PRO A 172 0 -0.30
CISPEP 2 ASN A 255 PRO A 256 0 -0.59
CISPEP 3 SER B 171 PRO B 172 0 2.67
CISPEP 4 ASN B 255 PRO B 256 0 -0.79
CRYST1 78.424 117.900 91.571 90.00 113.93 90.00 C 1 2 1 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 0.012751 0.000000 0.005660 0.00000
SCALE2 0.000000 0.008482 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011948 0.00000
(ATOM LINES ARE NOT SHOWN.)
END