HEADER TRANSFERASE 30-MAY-07 2Q3C
TITLE 2.1 A RESOLUTION CRYSTAL STRUCTURE OF O-ACETYLSERINE SULFHYDRYLASE
TITLE 2 (OASS) HOLOENZYME FROM MYCOBACTERIUM TUBERCULOSIS IN COMPLEX WITH THE
TITLE 3 INHIBITORY PEPTIDE DFSI
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CYSTEINE SYNTHASE A;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: O-ACETYLSERINE SULFHYDRYLASE A, O-ACETYLSERINE THIOL, LYASE
COMPND 5 A, CSASE A;
COMPND 6 EC: 2.5.1.47;
COMPND 7 ENGINEERED: YES;
COMPND 8 MOL_ID: 2;
COMPND 9 MOLECULE: DFSI INHIBITORY PEPTIDE;
COMPND 10 CHAIN: B;
COMPND 11 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MYCOBACTERIUM TUBERCULOSIS;
SOURCE 3 ORGANISM_TAXID: 1773;
SOURCE 4 STRAIN: RV2334;
SOURCE 5 GENE: CYSK;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET28A;
SOURCE 11 MOL_ID: 2;
SOURCE 12 SYNTHETIC: YES;
SOURCE 13 ORGANISM_SCIENTIFIC: MYCOBACTERIUM TUBERCULOSIS;
SOURCE 14 ORGANISM_TAXID: 1773
KEYWDS MYCOBACTERIUM TUBERCULOSIS, PYRIDOXAL-5'-PHOSPHATE, SULPHUR
KEYWDS 2 METABOLISM, CYSTEINE BIOSYNTHESIS, SAT, PEPTIDE-INHIBITOR,
KEYWDS 3 TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR G.SCHNEIDER,R.SCHNELL
REVDAT 6 15-NOV-23 2Q3C 1 REMARK
REVDAT 5 30-AUG-23 2Q3C 1 REMARK SEQADV LINK
REVDAT 4 02-APR-14 2Q3C 1 SOURCE
REVDAT 3 24-FEB-09 2Q3C 1 VERSN
REVDAT 2 21-AUG-07 2Q3C 1 JRNL
REVDAT 1 12-JUN-07 2Q3C 0
JRNL AUTH R.SCHNELL,W.OEHLMANN,M.SINGH,G.SCHNEIDER
JRNL TITL STRUCTURAL INSIGHTS INTO CATALYSIS AND INHIBITION OF
JRNL TITL 2 O-ACETYLSERINE SULFHYDRYLASE FROM MYCOBACTERIUM
JRNL TITL 3 TUBERCULOSIS: CRYSTAL STRUCTURES OF THE ENZYME
JRNL TITL 4 {ALPHA}-AMINOACRYLATE INTERMEDIATE AND AN ENZYME-INHIBITOR
JRNL TITL 5 COMPLEX.
JRNL REF J.BIOL.CHEM. V. 282 23473 2007
JRNL REFN ISSN 0021-9258
JRNL PMID 17567578
JRNL DOI 10.1074/JBC.M703518200
REMARK 2
REMARK 2 RESOLUTION. 2.10 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0005
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) : 2.10
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 51.23
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 92.3
REMARK 3 NUMBER OF REFLECTIONS : 25171
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) : 0.188
REMARK 3 R VALUE (WORKING SET) : 0.187
REMARK 3 FREE R VALUE : 0.207
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 1341
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) : 2.10
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.16
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1891
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 95.86
REMARK 3 BIN R VALUE (WORKING SET) : 0.2670
REMARK 3 BIN FREE R VALUE SET COUNT : 101
REMARK 3 BIN FREE R VALUE : 0.2960
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2276
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 8
REMARK 3 SOLVENT ATOMS : 163
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 31.00
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 36.73
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 1.94000
REMARK 3 B22 (A**2) : 1.94000
REMARK 3 B33 (A**2) : -3.89000
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): 0.165
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.142
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.108
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.219
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.959
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.944
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2331 ; 0.009 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): 14 ; 0.003 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3173 ; 1.195 ; 1.997
REMARK 3 BOND ANGLES OTHERS (DEGREES): 28 ; 6.900 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 306 ; 4.835 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 93 ;33.041 ;23.871
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 387 ;12.736 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 21 ;16.614 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 375 ; 0.130 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1749 ; 0.004 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 1112 ; 0.192 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): 8 ; 0.093 ; 0.200
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 1617 ; 0.299 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): 5 ; 0.047 ; 0.200
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 187 ; 0.140 ; 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): 49 ; 0.216 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 11 ; 0.109 ; 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): 1558 ; 0.587 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2441 ; 1.002 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 853 ; 1.588 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 730 ; 2.818 ; 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 : BABINET MODEL WITH 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 2Q3C COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 31-MAY-07.
REMARK 100 THE DEPOSITION ID IS D_1000043096.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 03-MAR-07
REMARK 200 TEMPERATURE (KELVIN) : 110
REMARK 200 PH : 8.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID14-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.934
REMARK 200 MONOCHROMATOR : DIAMOND(111), GE(220)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 210
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 26571
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.100
REMARK 200 RESOLUTION RANGE LOW (A) : 59.660
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 93.2
REMARK 200 DATA REDUNDANCY : 5.100
REMARK 200 R MERGE (I) : 0.08900
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 11.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.10
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.21
REMARK 200 COMPLETENESS FOR SHELL (%) : 96.2
REMARK 200 DATA REDUNDANCY IN SHELL : 5.00
REMARK 200 R MERGE FOR SHELL (I) : 0.35200
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.300
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: PDB ENTRY 2Q3B, HOLOENZYME
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 65.96
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.61
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M HEPES, 80% MPD, 4 MM DFSI
REMARK 280 -PEPTIDE, PH 8.0, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -Y+1/2,X+1/2,Z+1/4
REMARK 290 4555 Y+1/2,-X+1/2,Z+3/4
REMARK 290 5555 -X+1/2,Y+1/2,-Z+1/4
REMARK 290 6555 X+1/2,-Y+1/2,-Z+3/4
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -Y,-X,-Z+1/2
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 89.46800
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 36.22900
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 36.22900
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 44.73400
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 36.22900
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 36.22900
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 134.20200
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 36.22900
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 36.22900
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 44.73400
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 36.22900
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 36.22900
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 134.20200
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 89.46800
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 OASS FORMS A DIMER, THE SECOND PART OF THE BIOLOGICAL
REMARK 300 ASSEMBLY IS GENERATED BY THE TWO FOLD AXIS: -Y, X, -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 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 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 1.000000 0.000000 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 GLY A -2
REMARK 465 SER A -1
REMARK 465 HIS A 0
REMARK 465 SER A 301
REMARK 465 THR A 302
REMARK 465 PRO A 303
REMARK 465 LEU A 304
REMARK 465 PHE A 305
REMARK 465 ALA A 306
REMARK 465 ASP A 307
REMARK 465 VAL A 308
REMARK 465 ALA A 309
REMARK 465 ASP A 310
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 O HOH A 459 O HOH A 460 2.19
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 23 23.21 -148.10
REMARK 500 THR A 157 -72.56 -112.49
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MPD A 311
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2Q3B RELATED DB: PDB
REMARK 900 RELATED ID: 2Q3D RELATED DB: PDB
DBREF 2Q3C A 1 310 UNP P0A534 CYSK_MYCTU 1 310
DBREF 2Q3C B 1 4 PDB 2Q3C 2Q3C 1 4
SEQADV 2Q3C GLY A -2 UNP P0A534 CLONING ARTIFACT
SEQADV 2Q3C SER A -1 UNP P0A534 CLONING ARTIFACT
SEQADV 2Q3C HIS A 0 UNP P0A534 CLONING ARTIFACT
SEQRES 1 A 313 GLY SER HIS MET SER ILE ALA GLU ASP ILE THR GLN LEU
SEQRES 2 A 313 ILE GLY ARG THR PRO LEU VAL ARG LEU ARG ARG VAL THR
SEQRES 3 A 313 ASP GLY ALA VAL ALA ASP ILE VAL ALA LYS LEU GLU PHE
SEQRES 4 A 313 PHE ASN PRO ALA ASN SER VAL LLP ASP ARG ILE GLY VAL
SEQRES 5 A 313 ALA MET LEU GLN ALA ALA GLU GLN ALA GLY LEU ILE LYS
SEQRES 6 A 313 PRO ASP THR ILE ILE LEU GLU PRO THR SER GLY ASN THR
SEQRES 7 A 313 GLY ILE ALA LEU ALA MET VAL CYS ALA ALA ARG GLY TYR
SEQRES 8 A 313 ARG CYS VAL LEU THR MET PRO GLU THR MET SER LEU GLU
SEQRES 9 A 313 ARG ARG MET LEU LEU ARG ALA TYR GLY ALA GLU LEU ILE
SEQRES 10 A 313 LEU THR PRO GLY ALA ASP GLY MET SER GLY ALA ILE ALA
SEQRES 11 A 313 LYS ALA GLU GLU LEU ALA LYS THR ASP GLN ARG TYR PHE
SEQRES 12 A 313 VAL PRO GLN GLN PHE GLU ASN PRO ALA ASN PRO ALA ILE
SEQRES 13 A 313 HIS ARG VAL THR THR ALA GLU GLU VAL TRP ARG ASP THR
SEQRES 14 A 313 ASP GLY LYS VAL ASP ILE VAL VAL ALA GLY VAL GLY THR
SEQRES 15 A 313 GLY GLY THR ILE THR GLY VAL ALA GLN VAL ILE LYS GLU
SEQRES 16 A 313 ARG LYS PRO SER ALA ARG PHE VAL ALA VAL GLU PRO ALA
SEQRES 17 A 313 ALA SER PRO VAL LEU SER GLY GLY GLN LYS GLY PRO HIS
SEQRES 18 A 313 PRO ILE GLN GLY ILE GLY ALA GLY PHE VAL PRO PRO VAL
SEQRES 19 A 313 LEU ASP GLN ASP LEU VAL ASP GLU ILE ILE THR VAL GLY
SEQRES 20 A 313 ASN GLU ASP ALA LEU ASN VAL ALA ARG ARG LEU ALA ARG
SEQRES 21 A 313 GLU GLU GLY LEU LEU VAL GLY ILE SER SER GLY ALA ALA
SEQRES 22 A 313 THR VAL ALA ALA LEU GLN VAL ALA ARG ARG PRO GLU ASN
SEQRES 23 A 313 ALA GLY LYS LEU ILE VAL VAL VAL LEU PRO ASP PHE GLY
SEQRES 24 A 313 GLU ARG TYR LEU SER THR PRO LEU PHE ALA ASP VAL ALA
SEQRES 25 A 313 ASP
SEQRES 1 B 4 ASP PHE SER ILE
MODRES 2Q3C LLP A 44 LYS
HET LLP A 44 24
HET MPD A 311 8
HETNAM LLP (2S)-2-AMINO-6-[[3-HYDROXY-2-METHYL-5-
HETNAM 2 LLP (PHOSPHONOOXYMETHYL)PYRIDIN-4-
HETNAM 3 LLP YL]METHYLIDENEAMINO]HEXANOIC ACID
HETNAM MPD (4S)-2-METHYL-2,4-PENTANEDIOL
HETSYN LLP N'-PYRIDOXYL-LYSINE-5'-MONOPHOSPHATE
FORMUL 1 LLP C14 H22 N3 O7 P
FORMUL 3 MPD C6 H14 O2
FORMUL 4 HOH *163(H2 O)
HELIX 1 1 ASP A 6 ILE A 11 5 6
HELIX 2 2 PHE A 36 ASN A 38 5 3
HELIX 3 3 VAL A 43 ALA A 58 1 16
HELIX 4 4 GLY A 73 GLY A 87 1 15
HELIX 5 5 SER A 99 TYR A 109 1 11
HELIX 6 6 PRO A 117 ALA A 119 5 3
HELIX 7 7 ASP A 120 ASP A 136 1 17
HELIX 8 8 PRO A 148 THR A 157 1 10
HELIX 9 9 THR A 157 THR A 166 1 10
HELIX 10 10 GLY A 180 LYS A 194 1 15
HELIX 11 11 GLY A 244 GLY A 260 1 17
HELIX 12 12 GLY A 264 ARG A 279 1 16
HELIX 13 13 ARG A 280 ALA A 284 5 5
HELIX 14 14 PHE A 295 LEU A 300 5 6
SHEET 1 A 6 LEU A 16 ARG A 18 0
SHEET 2 A 6 ASP A 29 LEU A 34 -1 O ALA A 32 N VAL A 17
SHEET 3 A 6 LEU A 287 LEU A 292 1 O ILE A 288 N ASP A 29
SHEET 4 A 6 ILE A 172 GLY A 176 1 N ILE A 172 O VAL A 289
SHEET 5 A 6 ARG A 198 PRO A 204 1 O VAL A 200 N VAL A 173
SHEET 6 A 6 GLU A 239 VAL A 243 1 O GLU A 239 N ALA A 201
SHEET 1 B 4 GLU A 112 THR A 116 0
SHEET 2 B 4 ARG A 89 PRO A 95 1 N LEU A 92 O GLU A 112
SHEET 3 B 4 ILE A 66 PRO A 70 1 N ILE A 67 O VAL A 91
SHEET 4 B 4 TYR A 139 PHE A 140 1 O PHE A 140 N ILE A 66
LINK C VAL A 43 N LLP A 44 1555 1555 1.33
LINK C LLP A 44 N ASP A 45 1555 1555 1.34
SITE 1 AC1 3 VAL A 263 TYR A 299 HOH A 360
CRYST1 72.458 72.458 178.936 90.00 90.00 90.00 P 41 21 2 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 0.013801 0.000000 0.000000 0.00000
SCALE2 0.000000 0.013801 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005589 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
