HEADER TRANSFERASE 01-JUL-15 5CC7
TITLE CRYSTAL STRUCTURE OF MYCOBACTERIUM TUBERCULOSIS MALATE SYNTHASE IN
TITLE 2 COMPLEX WITH 1H-INDOLE-6-CARBOXYLIC ACID
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: MALATE SYNTHASE G;
COMPND 3 CHAIN: A;
COMPND 4 EC: 2.3.3.9;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MYCOBACTERIUM TUBERCULOSIS (STRAIN ATCC 25618 /
SOURCE 3 H37RV);
SOURCE 4 ORGANISM_TAXID: 83332;
SOURCE 5 STRAIN: ATCC 25618 / H37RV;
SOURCE 6 GENE: GLCB, RV1837C, MTCY1A11.06;
SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 9 EXPRESSION_SYSTEM_STRAIN: BL21
KEYWDS COMPLEX, FRAGMENT, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR H.-L.HUANG,J.C.SACCHETTINI
REVDAT 3 27-SEP-23 5CC7 1 REMARK
REVDAT 2 27-SEP-17 5CC7 1 REMARK
REVDAT 1 10-AUG-16 5CC7 0
JRNL AUTH H.-L.HUANG,I.V.KRIEGER,V.B.GAWANDI,M.PARAI,J.C.SACCHETTINI
JRNL TITL CRYSTAL STRUCTURES OF FRAGMENT-BOUND MALATE SYNTHASE FROM
JRNL TITL 2 MYCOBACTERIUM TUBERCULOSIS PROVIDE INSIGHTS INTO MECHANISM
JRNL TITL 3 AND POTENTIAL INHIBITOR DESIGNS
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH C.V.SMITH,C.C.HUANG,A.MICZAK,D.G.RUSSELL,J.C.SACCHETTINI,
REMARK 1 AUTH 2 K.HONER ZU BENTRUP
REMARK 1 TITL BIOCHEMICAL AND STRUCTURAL STUDIES OF MALATE SYNTHASE FROM
REMARK 1 TITL 2 MYCOBACTERIUM TUBERCULOSIS.
REMARK 1 REF J.BIOL.CHEM. V. 278 1735 2003
REMARK 1 REFN ISSN 0021-9258
REMARK 1 PMID 12393860
REMARK 1 DOI 10.1074/JBC.M209248200
REMARK 1 REFERENCE 2
REMARK 1 AUTH I.V.KRIEGER,J.S.FREUNDLICH,V.B.GAWANDI,J.P.ROBERTS,
REMARK 1 AUTH 2 V.B.GAWANDI,Q.SUN,J.L.OWEN,M.T.FRAILE,S.I.HUSS,
REMARK 1 AUTH 3 J.L.LAVANDERA,T.R.IOERGER,J.C.SACCHETTINI
REMARK 1 TITL STRUCTURE-GUIDED DISCOVERY OF PHENYL-DIKETO ACIDS AS POTENT
REMARK 1 TITL 2 INHIBITORS OF M. TUBERCULOSIS MALATE SYNTHASE.
REMARK 1 REF CHEM.BIOL. V. 19 1556 2012
REMARK 1 REFN ISSN 1074-5521
REMARK 1 PMID 23261599
REMARK 1 DOI 10.1016/J.CHEMBIOL.2012.09.018
REMARK 2
REMARK 2 RESOLUTION. 2.12 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC CCP4 6.5
REMARK 3 AUTHORS : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.12
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 45.10
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 96.5
REMARK 3 NUMBER OF REFLECTIONS : 40590
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : FREE R-VALUE
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM SELECTION
REMARK 3 R VALUE (WORKING + TEST SET) : NULL
REMARK 3 R VALUE (WORKING SET) : 0.189
REMARK 3 FREE R VALUE : 0.252
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 5393
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 13
REMARK 3 SOLVENT ATOMS : 726
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 26.78
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 32.26
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 4.99800
REMARK 3 B22 (A**2) : 4.99800
REMARK 3 B33 (A**2) : -9.99500
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): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): NULL
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): NULL
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 DISTANCE RESTRAINTS. RMS SIGMA
REMARK 3 BOND LENGTH (A) : NULL ; NULL
REMARK 3 ANGLE DISTANCE (A) : NULL ; NULL
REMARK 3 INTRAPLANAR 1-4 DISTANCE (A) : NULL ; NULL
REMARK 3 H-BOND OR METAL COORDINATION (A) : NULL ; NULL
REMARK 3
REMARK 3 PLANE RESTRAINT (A) : NULL ; NULL
REMARK 3 CHIRAL-CENTER RESTRAINT (A**3) : NULL ; NULL
REMARK 3
REMARK 3 NON-BONDED CONTACT RESTRAINTS.
REMARK 3 SINGLE TORSION (A) : NULL ; NULL
REMARK 3 MULTIPLE TORSION (A) : NULL ; NULL
REMARK 3 H-BOND (X...Y) (A) : NULL ; NULL
REMARK 3 H-BOND (X-H...Y) (A) : NULL ; NULL
REMARK 3
REMARK 3 CONFORMATIONAL TORSION ANGLE RESTRAINTS.
REMARK 3 SPECIFIED (DEGREES) : NULL ; NULL
REMARK 3 PLANAR (DEGREES) : NULL ; NULL
REMARK 3 STAGGERED (DEGREES) : NULL ; NULL
REMARK 3 TRANSVERSE (DEGREES) : NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 5CC7 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 02-JUL-15.
REMARK 100 THE DEPOSITION ID IS D_1000211276.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 19-OCT-13
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.0-8.5
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 23-ID-B
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.987
REMARK 200 MONOCHROMATOR : SI(111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 300 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 40595
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.120
REMARK 200 RESOLUTION RANGE LOW (A) : 45.100
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.3
REMARK 200 DATA REDUNDANCY : 7.600
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 24.5900
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.12
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.15
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.0
REMARK 200 DATA REDUNDANCY IN SHELL : 9.80
REMARK 200 R MERGE FOR SHELL (I) : NULL
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: MOLREP CCP4 6.5
REMARK 200 STARTING MODEL: 1N8I
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 44.76
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.23
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 3350, MAGNESIUM CHLORIDE, TRIS, PH
REMARK 280 7.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 300K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43 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+3/4
REMARK 290 4555 Y+1/2,-X+1/2,Z+1/4
REMARK 290 5555 -X+1/2,Y+1/2,-Z+3/4
REMARK 290 6555 X+1/2,-Y+1/2,-Z+1/4
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 112.91700
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 39.83050
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 39.83050
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 169.37550
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 39.83050
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 39.83050
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 56.45850
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 39.83050
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 39.83050
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 169.37550
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 39.83050
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 39.83050
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 56.45850
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 112.91700
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 110 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 26650 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -8.0 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 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 VAL A 72
REMARK 465 ILE A 73
REMARK 465 GLU A 74
REMARK 465 ALA A 302
REMARK 465 VAL A 303
REMARK 465 ASP A 304
REMARK 465 LYS A 305
REMARK 465 ASP A 306
REMARK 465 GLY A 307
REMARK 465 THR A 308
REMARK 465 ALA A 309
REMARK 465 PHE A 310
REMARK 465 LEU A 311
REMARK 465 VAL A 381
REMARK 465 ASN A 382
REMARK 465 GLY A 383
REMARK 465 PRO A 384
REMARK 465 LEU A 385
REMARK 465 ALA A 674
REMARK 465 GLY A 675
REMARK 465 ASP A 676
REMARK 465 VAL A 677
REMARK 465 LYS A 728
REMARK 465 PRO A 729
REMARK 465 ALA A 730
REMARK 465 PRO A 731
REMARK 465 SER A 732
REMARK 465 ASP A 733
REMARK 465 ARG A 734
REMARK 465 ALA A 735
REMARK 465 GLY A 736
REMARK 465 ASP A 737
REMARK 465 ASP A 738
REMARK 465 ALA A 739
REMARK 465 ALA A 740
REMARK 465 ARG A 741
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 1216 O HOH A 1446 1.97
REMARK 500 O HOH A 1205 O HOH A 1330 2.03
REMARK 500 O HOH A 945 O HOH A 1050 2.15
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 O HOH A 972 O HOH A 1357 8675 2.06
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 ASP A 3 59.94 -103.03
REMARK 500 GLU A 150 31.80 -82.43
REMARK 500 ASP A 152 129.13 -38.78
REMARK 500 HIS A 235 29.68 49.76
REMARK 500 ASP A 244 88.40 -153.33
REMARK 500 SER A 264 -88.37 -117.85
REMARK 500 GLU A 273 -115.66 -102.27
REMARK 500 ASN A 387 -108.17 -111.45
REMARK 500 GLU A 434 14.90 -145.03
REMARK 500 PRO A 582 49.11 -78.15
REMARK 500 ASP A 624 -158.37 -82.70
REMARK 500 HIS A 626 2.55 -66.42
REMARK 500 MET A 631 -93.06 -70.39
REMARK 500 GLU A 632 168.63 69.60
REMARK 500 ASP A 633 -156.67 -146.04
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 PRO A 75 ILE A 76 -137.80
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH A1617 DISTANCE = 5.86 ANGSTROMS
REMARK 525 HOH A1618 DISTANCE = 6.19 ANGSTROMS
REMARK 525 HOH A1619 DISTANCE = 6.35 ANGSTROMS
REMARK 525 HOH A1620 DISTANCE = 6.38 ANGSTROMS
REMARK 525 HOH A1621 DISTANCE = 6.41 ANGSTROMS
REMARK 525 HOH A1622 DISTANCE = 6.54 ANGSTROMS
REMARK 525 HOH A1623 DISTANCE = 6.66 ANGSTROMS
REMARK 525 HOH A1624 DISTANCE = 6.66 ANGSTROMS
REMARK 525 HOH A1625 DISTANCE = 6.73 ANGSTROMS
REMARK 525 HOH A1626 DISTANCE = 6.82 ANGSTROMS
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 801 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 434 OE2
REMARK 620 2 ASP A 462 OD1 93.7
REMARK 620 3 HOH A 934 O 177.6 86.9
REMARK 620 4 HOH A 939 O 79.9 99.3 97.7
REMARK 620 5 HOH A1304 O 89.4 169.7 90.3 90.9
REMARK 620 6 HOH A1389 O 87.6 100.3 94.6 157.4 70.1
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 MG A 801
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 1F1 A 802
DBREF 5CC7 A 1 741 UNP P9WK17 MASZ_MYCTU 1 741
SEQADV 5CC7 ALA A 619 UNP P9WK17 CYS 619 ENGINEERED MUTATION
SEQRES 1 A 741 MET THR ASP ARG VAL SER VAL GLY ASN LEU ARG ILE ALA
SEQRES 2 A 741 ARG VAL LEU TYR ASP PHE VAL ASN ASN GLU ALA LEU PRO
SEQRES 3 A 741 GLY THR ASP ILE ASP PRO ASP SER PHE TRP ALA GLY VAL
SEQRES 4 A 741 ASP LYS VAL VAL ALA ASP LEU THR PRO GLN ASN GLN ALA
SEQRES 5 A 741 LEU LEU ASN ALA ARG ASP GLU LEU GLN ALA GLN ILE ASP
SEQRES 6 A 741 LYS TRP HIS ARG ARG ARG VAL ILE GLU PRO ILE ASP MET
SEQRES 7 A 741 ASP ALA TYR ARG GLN PHE LEU THR GLU ILE GLY TYR LEU
SEQRES 8 A 741 LEU PRO GLU PRO ASP ASP PHE THR ILE THR THR SER GLY
SEQRES 9 A 741 VAL ASP ALA GLU ILE THR THR THR ALA GLY PRO GLN LEU
SEQRES 10 A 741 VAL VAL PRO VAL LEU ASN ALA ARG PHE ALA LEU ASN ALA
SEQRES 11 A 741 ALA ASN ALA ARG TRP GLY SER LEU TYR ASP ALA LEU TYR
SEQRES 12 A 741 GLY THR ASP VAL ILE PRO GLU THR ASP GLY ALA GLU LYS
SEQRES 13 A 741 GLY PRO THR TYR ASN LYS VAL ARG GLY ASP LYS VAL ILE
SEQRES 14 A 741 ALA TYR ALA ARG LYS PHE LEU ASP ASP SER VAL PRO LEU
SEQRES 15 A 741 SER SER GLY SER PHE GLY ASP ALA THR GLY PHE THR VAL
SEQRES 16 A 741 GLN ASP GLY GLN LEU VAL VAL ALA LEU PRO ASP LYS SER
SEQRES 17 A 741 THR GLY LEU ALA ASN PRO GLY GLN PHE ALA GLY TYR THR
SEQRES 18 A 741 GLY ALA ALA GLU SER PRO THR SER VAL LEU LEU ILE ASN
SEQRES 19 A 741 HIS GLY LEU HIS ILE GLU ILE LEU ILE ASP PRO GLU SER
SEQRES 20 A 741 GLN VAL GLY THR THR ASP ARG ALA GLY VAL LYS ASP VAL
SEQRES 21 A 741 ILE LEU GLU SER ALA ILE THR THR ILE MET ASP PHE GLU
SEQRES 22 A 741 ASP SER VAL ALA ALA VAL ASP ALA ALA ASP LYS VAL LEU
SEQRES 23 A 741 GLY TYR ARG ASN TRP LEU GLY LEU ASN LYS GLY ASP LEU
SEQRES 24 A 741 ALA ALA ALA VAL ASP LYS ASP GLY THR ALA PHE LEU ARG
SEQRES 25 A 741 VAL LEU ASN ARG ASP ARG ASN TYR THR ALA PRO GLY GLY
SEQRES 26 A 741 GLY GLN PHE THR LEU PRO GLY ARG SER LEU MET PHE VAL
SEQRES 27 A 741 ARG ASN VAL GLY HIS LEU MET THR ASN ASP ALA ILE VAL
SEQRES 28 A 741 ASP THR ASP GLY SER GLU VAL PHE GLU GLY ILE MET ASP
SEQRES 29 A 741 ALA LEU PHE THR GLY LEU ILE ALA ILE HIS GLY LEU LYS
SEQRES 30 A 741 ALA SER ASP VAL ASN GLY PRO LEU ILE ASN SER ARG THR
SEQRES 31 A 741 GLY SER ILE TYR ILE VAL LYS PRO LYS MET HIS GLY PRO
SEQRES 32 A 741 ALA GLU VAL ALA PHE THR CYS GLU LEU PHE SER ARG VAL
SEQRES 33 A 741 GLU ASP VAL LEU GLY LEU PRO GLN ASN THR MET LYS ILE
SEQRES 34 A 741 GLY ILE MET ASP GLU GLU ARG ARG THR THR VAL ASN LEU
SEQRES 35 A 741 LYS ALA CYS ILE LYS ALA ALA ALA ASP ARG VAL VAL PHE
SEQRES 36 A 741 ILE ASN THR GLY PHE LEU ASP ARG THR GLY ASP GLU ILE
SEQRES 37 A 741 HIS THR SER MET GLU ALA GLY PRO MET VAL ARG LYS GLY
SEQRES 38 A 741 THR MET LYS SER GLN PRO TRP ILE LEU ALA TYR GLU ASP
SEQRES 39 A 741 HIS ASN VAL ASP ALA GLY LEU ALA ALA GLY PHE SER GLY
SEQRES 40 A 741 ARG ALA GLN VAL GLY LYS GLY MET TRP THR MET THR GLU
SEQRES 41 A 741 LEU MET ALA ASP MET VAL GLU THR LYS ILE ALA GLN PRO
SEQRES 42 A 741 ARG ALA GLY ALA SER THR ALA TRP VAL PRO SER PRO THR
SEQRES 43 A 741 ALA ALA THR LEU HIS ALA LEU HIS TYR HIS GLN VAL ASP
SEQRES 44 A 741 VAL ALA ALA VAL GLN GLN GLY LEU ALA GLY LYS ARG ARG
SEQRES 45 A 741 ALA THR ILE GLU GLN LEU LEU THR ILE PRO LEU ALA LYS
SEQRES 46 A 741 GLU LEU ALA TRP ALA PRO ASP GLU ILE ARG GLU GLU VAL
SEQRES 47 A 741 ASP ASN ASN CYS GLN SER ILE LEU GLY TYR VAL VAL ARG
SEQRES 48 A 741 TRP VAL ASP GLN GLY VAL GLY ALA SER LYS VAL PRO ASP
SEQRES 49 A 741 ILE HIS ASP VAL ALA LEU MET GLU ASP ARG ALA THR LEU
SEQRES 50 A 741 ARG ILE SER SER GLN LEU LEU ALA ASN TRP LEU ARG HIS
SEQRES 51 A 741 GLY VAL ILE THR SER ALA ASP VAL ARG ALA SER LEU GLU
SEQRES 52 A 741 ARG MET ALA PRO LEU VAL ASP ARG GLN ASN ALA GLY ASP
SEQRES 53 A 741 VAL ALA TYR ARG PRO MET ALA PRO ASN PHE ASP ASP SER
SEQRES 54 A 741 ILE ALA PHE LEU ALA ALA GLN GLU LEU ILE LEU SER GLY
SEQRES 55 A 741 ALA GLN GLN PRO ASN GLY TYR THR GLU PRO ILE LEU HIS
SEQRES 56 A 741 ARG ARG ARG ARG GLU PHE LYS ALA ARG ALA ALA GLU LYS
SEQRES 57 A 741 PRO ALA PRO SER ASP ARG ALA GLY ASP ASP ALA ALA ARG
HET MG A 801 1
HET 1F1 A 802 12
HETNAM MG MAGNESIUM ION
HETNAM 1F1 1H-INDOLE-6-CARBOXYLIC ACID
FORMUL 2 MG MG 2+
FORMUL 3 1F1 C9 H7 N O2
FORMUL 4 HOH *726(H2 O)
HELIX 1 AA1 ARG A 14 GLU A 23 1 10
HELIX 2 AA2 ASP A 31 ARG A 70 1 40
HELIX 3 AA3 ASP A 77 ILE A 88 1 12
HELIX 4 AA4 ASP A 106 THR A 111 1 6
HELIX 5 AA5 ASN A 123 ASN A 132 1 10
HELIX 6 AA6 LEU A 138 THR A 145 1 8
HELIX 7 AA7 ASN A 161 VAL A 180 1 20
HELIX 8 AA8 SER A 186 ALA A 190 5 5
HELIX 9 AA9 ASN A 213 GLY A 215 5 3
HELIX 10 AB1 SER A 247 ASP A 253 1 7
HELIX 11 AB2 ASP A 280 LYS A 296 1 17
HELIX 12 AB3 GLU A 360 ILE A 373 1 14
HELIX 13 AB4 HIS A 374 LYS A 377 5 4
HELIX 14 AB5 GLY A 402 GLY A 421 1 20
HELIX 15 AB6 GLU A 435 VAL A 440 1 6
HELIX 16 AB7 ASN A 441 ALA A 449 1 9
HELIX 17 AB8 GLY A 459 SER A 471 1 13
HELIX 18 AB9 ARG A 479 LYS A 484 1 6
HELIX 19 AC1 GLN A 486 ALA A 503 1 18
HELIX 20 AC2 LEU A 521 LYS A 529 1 9
HELIX 21 AC3 ILE A 530 ALA A 535 1 6
HELIX 22 AC4 SER A 544 VAL A 558 1 15
HELIX 23 AC5 ASP A 559 ALA A 568 1 10
HELIX 24 AC6 THR A 574 LEU A 579 1 6
HELIX 25 AC7 ALA A 590 GLY A 616 1 27
HELIX 26 AC8 ASP A 633 HIS A 650 1 18
HELIX 27 AC9 THR A 654 ASN A 673 1 20
HELIX 28 AD1 ASN A 685 ASP A 688 5 4
HELIX 29 AD2 SER A 689 SER A 701 1 13
HELIX 30 AD3 GLY A 702 TYR A 709 5 8
HELIX 31 AD4 THR A 710 GLU A 727 1 18
SHEET 1 AA1 4 ARG A 4 VAL A 7 0
SHEET 2 AA1 4 LEU A 10 ALA A 13 -1 O ILE A 12 N VAL A 5
SHEET 3 AA1 4 THR A 346 ASP A 352 -1 O VAL A 351 N ARG A 11
SHEET 4 AA1 4 GLU A 357 PHE A 359 -1 O VAL A 358 N ILE A 350
SHEET 1 AA2 9 GLN A 116 PRO A 120 0
SHEET 2 AA2 9 THR A 267 ASP A 271 1 O ILE A 269 N LEU A 117
SHEET 3 AA2 9 LEU A 335 ARG A 339 1 O PHE A 337 N THR A 268
SHEET 4 AA2 9 ILE A 393 LYS A 397 1 O VAL A 396 N VAL A 338
SHEET 5 AA2 9 MET A 427 ASP A 433 1 O LYS A 428 N ILE A 393
SHEET 6 AA2 9 VAL A 453 THR A 458 1 O ASN A 457 N ASP A 433
SHEET 7 AA2 9 GLN A 510 LYS A 513 1 O GLY A 512 N ILE A 456
SHEET 8 AA2 9 THR A 539 VAL A 542 1 O THR A 539 N LYS A 513
SHEET 9 AA2 9 GLN A 116 PRO A 120 1 N GLN A 116 O ALA A 540
SHEET 1 AA3 5 TRP A 135 SER A 137 0
SHEET 2 AA3 5 VAL A 257 GLU A 263 -1 O LEU A 262 N GLY A 136
SHEET 3 AA3 5 LEU A 237 ILE A 243 -1 N GLU A 240 O ILE A 261
SHEET 4 AA3 5 SER A 229 ASN A 234 -1 N LEU A 232 O ILE A 239
SHEET 5 AA3 5 PHE A 217 THR A 221 -1 N ALA A 218 O LEU A 231
SHEET 1 AA4 3 GLY A 192 GLN A 196 0
SHEET 2 AA4 3 GLN A 199 ALA A 203 -1 O VAL A 201 N THR A 194
SHEET 3 AA4 3 SER A 208 THR A 209 -1 O THR A 209 N VAL A 202
SHEET 1 AA5 2 ARG A 318 THR A 321 0
SHEET 2 AA5 2 GLN A 327 LEU A 330 -1 O LEU A 330 N ARG A 318
SHEET 1 AA6 2 VAL A 622 PRO A 623 0
SHEET 2 AA6 2 ALA A 629 LEU A 630 -1 O LEU A 630 N VAL A 622
LINK OE2 GLU A 434 MG MG A 801 1555 1555 2.29
LINK OD1 ASP A 462 MG MG A 801 1555 1555 2.19
LINK MG MG A 801 O HOH A 934 1555 1555 2.25
LINK MG MG A 801 O HOH A 939 1555 1555 2.30
LINK MG MG A 801 O HOH A1304 1555 1555 2.42
LINK MG MG A 801 O HOH A1389 1555 1555 2.41
CISPEP 1 ALA A 683 PRO A 684 0 -1.61
SITE 1 AC1 6 GLU A 434 ASP A 462 HOH A 934 HOH A 939
SITE 2 AC1 6 HOH A1304 HOH A1389
SITE 1 AC2 10 VAL A 118 SER A 275 ARG A 339 TRP A 541
SITE 2 AC2 10 MET A 631 ASP A 633 HOH A 934 HOH A1020
SITE 3 AC2 10 HOH A1023 HOH A1304
CRYST1 79.661 79.661 225.834 90.00 90.00 90.00 P 43 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 0.012553 0.000000 0.000000 0.00000
SCALE2 0.000000 0.012553 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004428 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
