HEADER TRANSFERASE/TRANSFERASE INHIBITOR 13-JUN-16 5KGT
TITLE CRYSTAL STRUCTURE OF 7,8-DIAMINOPELARGONIC ACID SYNTHASE (BIOA) FROM
TITLE 2 MYCOBACTERIUM TUBERCULOSIS, COMPLEXED WITH AN INHIBITOR OPTIMIZED
TITLE 3 FROM HTS LEAD: 1-[4-[4-(3-CHLOROPHENYL)CARBONYLPIPERIDIN-1-
TITLE 4 YL]PHENYL]ETHANONE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ADENOSYLMETHIONINE-8-AMINO-7-OXONONANOATE AMINOTRANSFERASE;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: 7,8-DIAMINO-PELARGONIC ACID AMINOTRANSFERASE,DAPA
COMPND 5 AMINOTRANSFERASE,8-DIAMINONONANOATE SYNTHASE,DANS,DIAMINOPELARGONIC
COMPND 6 ACID SYNTHASE;
COMPND 7 EC: 2.6.1.62;
COMPND 8 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MYCOBACTERIUM BOVIS (STRAIN ATCC BAA-935 /
SOURCE 3 AF2122/97);
SOURCE 4 ORGANISM_TAXID: 233413;
SOURCE 5 STRAIN: ATCC BAA-935 / AF2122/97;
SOURCE 6 GENE: BIOA, MB1595;
SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS TRANSAMINASE, PLP, TRANSFERASE, TRANSFERASE-INHIBITOR COMPLEX,
KEYWDS 2 TRANSFERASE-TRANSFERASE INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR K.M.MAIZE,A.DIVAKARAN,C.C.ALDRICH,B.C.FINZEL
REVDAT 7 27-SEP-23 5KGT 1 REMARK
REVDAT 6 11-DEC-19 5KGT 1 REMARK
REVDAT 5 20-SEP-17 5KGT 1 REMARK
REVDAT 4 26-JUL-17 5KGT 1 JRNL
REVDAT 3 05-JUL-17 5KGT 1 JRNL
REVDAT 2 21-JUN-17 5KGT 1 JRNL
REVDAT 1 14-JUN-17 5KGT 0
JRNL AUTH F.LIU,S.DAWADI,K.M.MAIZE,R.DAI,S.W.PARK,D.SCHNAPPINGER,
JRNL AUTH 2 B.C.FINZEL,C.C.ALDRICH
JRNL TITL STRUCTURE-BASED OPTIMIZATION OF PYRIDOXAL
JRNL TITL 2 5'-PHOSPHATE-DEPENDENT TRANSAMINASE ENZYME (BIOA) INHIBITORS
JRNL TITL 3 THAT TARGET BIOTIN BIOSYNTHESIS IN MYCOBACTERIUM
JRNL TITL 4 TUBERCULOSIS.
JRNL REF J. MED. CHEM. V. 60 5507 2017
JRNL REFN ISSN 1520-4804
JRNL PMID 28594172
JRNL DOI 10.1021/ACS.JMEDCHEM.7B00189
REMARK 2
REMARK 2 RESOLUTION. 2.25 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.25
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 62.81
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 40983
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.174
REMARK 3 R VALUE (WORKING SET) : 0.171
REMARK 3 FREE R VALUE : 0.224
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.010
REMARK 3 FREE R VALUE TEST SET COUNT : 2052
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 62.8381 - 5.5479 1.00 2797 147 0.1495 0.1604
REMARK 3 2 5.5479 - 4.4039 1.00 2676 124 0.1368 0.1749
REMARK 3 3 4.4039 - 3.8473 1.00 2658 109 0.1397 0.1644
REMARK 3 4 3.8473 - 3.4956 1.00 2585 155 0.1681 0.2133
REMARK 3 5 3.4956 - 3.2450 1.00 2627 125 0.1831 0.2495
REMARK 3 6 3.2450 - 3.0537 1.00 2562 153 0.1923 0.2655
REMARK 3 7 3.0537 - 2.9008 1.00 2576 143 0.1905 0.2413
REMARK 3 8 2.9008 - 2.7745 1.00 2554 139 0.1930 0.2314
REMARK 3 9 2.7745 - 2.6677 1.00 2594 130 0.1919 0.2538
REMARK 3 10 2.6677 - 2.5757 1.00 2578 137 0.1852 0.2710
REMARK 3 11 2.5757 - 2.4951 1.00 2546 133 0.1937 0.2514
REMARK 3 12 2.4951 - 2.4238 1.00 2515 156 0.1909 0.2573
REMARK 3 13 2.4238 - 2.3600 1.00 2543 142 0.1983 0.2946
REMARK 3 14 2.3600 - 2.3024 1.00 2589 120 0.1827 0.2804
REMARK 3 15 2.3024 - 2.2501 1.00 2531 139 0.1827 0.2444
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.230
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 19.560
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 21.11
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 21.61
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.006 6612
REMARK 3 ANGLE : 0.877 9048
REMARK 3 CHIRALITY : 0.050 1038
REMARK 3 PLANARITY : 0.006 1166
REMARK 3 DIHEDRAL : 16.091 3842
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 5KGT COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 15-JUN-16.
REMARK 100 THE DEPOSITION ID IS D_1000222195.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 24-SEP-15
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 : ALS
REMARK 200 BEAMLINE : 4.2.2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.000
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CMOS
REMARK 200 DETECTOR MANUFACTURER : RDI CMOS_8M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : AIMLESS 0.5.9
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 41063
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.250
REMARK 200 RESOLUTION RANGE LOW (A) : 63.020
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 7.100
REMARK 200 R MERGE (I) : 0.10000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 17.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.25
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.32
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 6.50
REMARK 200 R MERGE FOR SHELL (I) : 0.39900
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: 4W1X
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 43.27
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.17
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM HEPES, 13% PEG 8000, PH 7.5,
REMARK 280 VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K
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 31.51200
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 101.07350
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 33.04250
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 101.07350
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 31.51200
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 33.04250
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: 10650 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 26540 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -82.0 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 -19
REMARK 465 GLY A -18
REMARK 465 SER A -17
REMARK 465 SER A -16
REMARK 465 HIS A -15
REMARK 465 HIS A -14
REMARK 465 HIS A -13
REMARK 465 HIS A -12
REMARK 465 HIS A -11
REMARK 465 HIS A -10
REMARK 465 SER A -9
REMARK 465 SER A -8
REMARK 465 GLY A -7
REMARK 465 LEU A -6
REMARK 465 VAL A -5
REMARK 465 PRO A -4
REMARK 465 ARG A -3
REMARK 465 GLY A -2
REMARK 465 SER A -1
REMARK 465 HIS A 0
REMARK 465 MET A 1
REMARK 465 ALA A 2
REMARK 465 ALA A 3
REMARK 465 ALA A 4
REMARK 465 THR A 5
REMARK 465 GLY A 6
REMARK 465 GLY A 7
REMARK 465 PRO A 437
REMARK 465 MET B -19
REMARK 465 GLY B -18
REMARK 465 SER B -17
REMARK 465 SER B -16
REMARK 465 HIS B -15
REMARK 465 HIS B -14
REMARK 465 HIS B -13
REMARK 465 HIS B -12
REMARK 465 HIS B -11
REMARK 465 HIS B -10
REMARK 465 SER B -9
REMARK 465 SER B -8
REMARK 465 GLY B -7
REMARK 465 LEU B -6
REMARK 465 VAL B -5
REMARK 465 PRO B -4
REMARK 465 ARG B -3
REMARK 465 GLY B -2
REMARK 465 SER B -1
REMARK 465 HIS B 0
REMARK 465 MET B 1
REMARK 465 ALA B 2
REMARK 465 ALA B 3
REMARK 465 ALA B 4
REMARK 465 THR B 5
REMARK 465 GLY B 6
REMARK 465 LEU B 436
REMARK 465 PRO B 437
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 MET A 174 CG SD CE
REMARK 470 LEU A 177 CG CD1 CD2
REMARK 470 ARG B 30 CG CD NE CZ NH1 NH2
REMARK 470 ARG B 50 CG CD NE CZ NH1 NH2
REMARK 470 GLU B 428 CG CD OE1 OE2
REMARK 480
REMARK 480 ZERO OCCUPANCY ATOM
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 480 M RES C SSEQI ATOMS
REMARK 480 ARG A 403 CZ
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 TYR A 25 52.74 38.67
REMARK 500 MET A 87 109.29 -174.10
REMARK 500 HIS A 89 139.58 -174.28
REMARK 500 HIS A 158 16.49 -141.36
REMARK 500 ASP A 180 -19.22 71.63
REMARK 500 VAL A 222 -44.79 72.93
REMARK 500 ALA A 373 43.45 -83.31
REMARK 500 ARG A 403 -123.31 51.66
REMARK 500 SER A 435 -94.55 -85.29
REMARK 500 TRP B 65 5.13 80.09
REMARK 500 MET B 87 106.41 -167.57
REMARK 500 HIS B 89 143.50 -172.74
REMARK 500 VAL B 181 -58.79 -120.94
REMARK 500 VAL B 222 -51.44 72.14
REMARK 500 ARG B 403 -125.76 49.89
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 A 738 DISTANCE = 5.95 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PLP A 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 6SQ B 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide PLP B 502 and LYS B
REMARK 800 283
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4W1X RELATED DB: PDB
REMARK 900 RELATED ID: 4WY4 RELATED DB: PDB
REMARK 900 RELATED ID: 4XJO RELATED DB: PDB
REMARK 900 RELATED ID: 4XJP RELATED DB: PDB
REMARK 900 RELATED ID: 5KGS RELATED DB: PDB
DBREF 5KGT A 1 437 UNP P0A4X7 BIOA_MYCBO 1 437
DBREF 5KGT B 1 437 UNP P0A4X7 BIOA_MYCBO 1 437
SEQADV 5KGT MET A -19 UNP P0A4X7 INITIATING METHIONINE
SEQADV 5KGT GLY A -18 UNP P0A4X7 EXPRESSION TAG
SEQADV 5KGT SER A -17 UNP P0A4X7 EXPRESSION TAG
SEQADV 5KGT SER A -16 UNP P0A4X7 EXPRESSION TAG
SEQADV 5KGT HIS A -15 UNP P0A4X7 EXPRESSION TAG
SEQADV 5KGT HIS A -14 UNP P0A4X7 EXPRESSION TAG
SEQADV 5KGT HIS A -13 UNP P0A4X7 EXPRESSION TAG
SEQADV 5KGT HIS A -12 UNP P0A4X7 EXPRESSION TAG
SEQADV 5KGT HIS A -11 UNP P0A4X7 EXPRESSION TAG
SEQADV 5KGT HIS A -10 UNP P0A4X7 EXPRESSION TAG
SEQADV 5KGT SER A -9 UNP P0A4X7 EXPRESSION TAG
SEQADV 5KGT SER A -8 UNP P0A4X7 EXPRESSION TAG
SEQADV 5KGT GLY A -7 UNP P0A4X7 EXPRESSION TAG
SEQADV 5KGT LEU A -6 UNP P0A4X7 EXPRESSION TAG
SEQADV 5KGT VAL A -5 UNP P0A4X7 EXPRESSION TAG
SEQADV 5KGT PRO A -4 UNP P0A4X7 EXPRESSION TAG
SEQADV 5KGT ARG A -3 UNP P0A4X7 EXPRESSION TAG
SEQADV 5KGT GLY A -2 UNP P0A4X7 EXPRESSION TAG
SEQADV 5KGT SER A -1 UNP P0A4X7 EXPRESSION TAG
SEQADV 5KGT HIS A 0 UNP P0A4X7 EXPRESSION TAG
SEQADV 5KGT MET B -19 UNP P0A4X7 INITIATING METHIONINE
SEQADV 5KGT GLY B -18 UNP P0A4X7 EXPRESSION TAG
SEQADV 5KGT SER B -17 UNP P0A4X7 EXPRESSION TAG
SEQADV 5KGT SER B -16 UNP P0A4X7 EXPRESSION TAG
SEQADV 5KGT HIS B -15 UNP P0A4X7 EXPRESSION TAG
SEQADV 5KGT HIS B -14 UNP P0A4X7 EXPRESSION TAG
SEQADV 5KGT HIS B -13 UNP P0A4X7 EXPRESSION TAG
SEQADV 5KGT HIS B -12 UNP P0A4X7 EXPRESSION TAG
SEQADV 5KGT HIS B -11 UNP P0A4X7 EXPRESSION TAG
SEQADV 5KGT HIS B -10 UNP P0A4X7 EXPRESSION TAG
SEQADV 5KGT SER B -9 UNP P0A4X7 EXPRESSION TAG
SEQADV 5KGT SER B -8 UNP P0A4X7 EXPRESSION TAG
SEQADV 5KGT GLY B -7 UNP P0A4X7 EXPRESSION TAG
SEQADV 5KGT LEU B -6 UNP P0A4X7 EXPRESSION TAG
SEQADV 5KGT VAL B -5 UNP P0A4X7 EXPRESSION TAG
SEQADV 5KGT PRO B -4 UNP P0A4X7 EXPRESSION TAG
SEQADV 5KGT ARG B -3 UNP P0A4X7 EXPRESSION TAG
SEQADV 5KGT GLY B -2 UNP P0A4X7 EXPRESSION TAG
SEQADV 5KGT SER B -1 UNP P0A4X7 EXPRESSION TAG
SEQADV 5KGT HIS B 0 UNP P0A4X7 EXPRESSION TAG
SEQRES 1 A 457 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 A 457 LEU VAL PRO ARG GLY SER HIS MET ALA ALA ALA THR GLY
SEQRES 3 A 457 GLY LEU THR PRO GLU GLN ILE ILE ALA VAL ASP GLY ALA
SEQRES 4 A 457 HIS LEU TRP HIS PRO TYR SER SER ILE GLY ARG GLU ALA
SEQRES 5 A 457 VAL SER PRO VAL VAL ALA VAL ALA ALA HIS GLY ALA TRP
SEQRES 6 A 457 LEU THR LEU ILE ARG ASP GLY GLN PRO ILE GLU VAL LEU
SEQRES 7 A 457 ASP ALA MET SER SER TRP TRP THR ALA ILE HIS GLY HIS
SEQRES 8 A 457 GLY HIS PRO ALA LEU ASP GLN ALA LEU THR THR GLN LEU
SEQRES 9 A 457 ARG VAL MET ASN HIS VAL MET PHE GLY GLY LEU THR HIS
SEQRES 10 A 457 GLU PRO ALA ALA ARG LEU ALA LYS LEU LEU VAL ASP ILE
SEQRES 11 A 457 THR PRO ALA GLY LEU ASP THR VAL PHE PHE SER ASP SER
SEQRES 12 A 457 GLY SER VAL SER VAL GLU VAL ALA ALA LYS MET ALA LEU
SEQRES 13 A 457 GLN TYR TRP ARG GLY ARG GLY LEU PRO GLY LYS ARG ARG
SEQRES 14 A 457 LEU MET THR TRP ARG GLY GLY TYR HIS GLY ASP THR PHE
SEQRES 15 A 457 LEU ALA MET SER ILE CYS ASP PRO HIS GLY GLY MET HIS
SEQRES 16 A 457 SER LEU TRP THR ASP VAL LEU ALA ALA GLN VAL PHE ALA
SEQRES 17 A 457 PRO GLN VAL PRO ARG ASP TYR ASP PRO ALA TYR SER ALA
SEQRES 18 A 457 ALA PHE GLU ALA GLN LEU ALA GLN HIS ALA GLY GLU LEU
SEQRES 19 A 457 ALA ALA VAL VAL VAL GLU PRO VAL VAL GLN GLY ALA GLY
SEQRES 20 A 457 GLY MET ARG PHE HIS ASP PRO ARG TYR LEU HIS ASP LEU
SEQRES 21 A 457 ARG ASP ILE CYS ARG ARG TYR GLU VAL LEU LEU ILE PHE
SEQRES 22 A 457 ASP GLU ILE ALA THR GLY PHE GLY ARG THR GLY ALA LEU
SEQRES 23 A 457 PHE ALA ALA ASP HIS ALA GLY VAL SER PRO ASP ILE MET
SEQRES 24 A 457 CYS VAL GLY LYS ALA LEU THR GLY GLY TYR LEU SER LEU
SEQRES 25 A 457 ALA ALA THR LEU CYS THR ALA ASP VAL ALA HIS THR ILE
SEQRES 26 A 457 SER ALA GLY ALA ALA GLY ALA LEU MET HIS GLY PRO THR
SEQRES 27 A 457 PHE MET ALA ASN PRO LEU ALA CYS ALA VAL SER VAL ALA
SEQRES 28 A 457 SER VAL GLU LEU LEU LEU GLY GLN ASP TRP ARG THR ARG
SEQRES 29 A 457 ILE THR GLU LEU ALA ALA GLY LEU THR ALA GLY LEU ASP
SEQRES 30 A 457 THR ALA ARG ALA LEU PRO ALA VAL THR ASP VAL ARG VAL
SEQRES 31 A 457 CYS GLY ALA ILE GLY VAL ILE GLU CYS ASP ARG PRO VAL
SEQRES 32 A 457 ASP LEU ALA VAL ALA THR PRO ALA ALA LEU ASP ARG GLY
SEQRES 33 A 457 VAL TRP LEU ARG PRO PHE ARG ASN LEU VAL TYR ALA MET
SEQRES 34 A 457 PRO PRO TYR ILE CYS THR PRO ALA GLU ILE THR GLN ILE
SEQRES 35 A 457 THR SER ALA MET VAL GLU VAL ALA ARG LEU VAL GLY SER
SEQRES 36 A 457 LEU PRO
SEQRES 1 B 457 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 B 457 LEU VAL PRO ARG GLY SER HIS MET ALA ALA ALA THR GLY
SEQRES 3 B 457 GLY LEU THR PRO GLU GLN ILE ILE ALA VAL ASP GLY ALA
SEQRES 4 B 457 HIS LEU TRP HIS PRO TYR SER SER ILE GLY ARG GLU ALA
SEQRES 5 B 457 VAL SER PRO VAL VAL ALA VAL ALA ALA HIS GLY ALA TRP
SEQRES 6 B 457 LEU THR LEU ILE ARG ASP GLY GLN PRO ILE GLU VAL LEU
SEQRES 7 B 457 ASP ALA MET SER SER TRP TRP THR ALA ILE HIS GLY HIS
SEQRES 8 B 457 GLY HIS PRO ALA LEU ASP GLN ALA LEU THR THR GLN LEU
SEQRES 9 B 457 ARG VAL MET ASN HIS VAL MET PHE GLY GLY LEU THR HIS
SEQRES 10 B 457 GLU PRO ALA ALA ARG LEU ALA LYS LEU LEU VAL ASP ILE
SEQRES 11 B 457 THR PRO ALA GLY LEU ASP THR VAL PHE PHE SER ASP SER
SEQRES 12 B 457 GLY SER VAL SER VAL GLU VAL ALA ALA LYS MET ALA LEU
SEQRES 13 B 457 GLN TYR TRP ARG GLY ARG GLY LEU PRO GLY LYS ARG ARG
SEQRES 14 B 457 LEU MET THR TRP ARG GLY GLY TYR HIS GLY ASP THR PHE
SEQRES 15 B 457 LEU ALA MET SER ILE CYS ASP PRO HIS GLY GLY MET HIS
SEQRES 16 B 457 SER LEU TRP THR ASP VAL LEU ALA ALA GLN VAL PHE ALA
SEQRES 17 B 457 PRO GLN VAL PRO ARG ASP TYR ASP PRO ALA TYR SER ALA
SEQRES 18 B 457 ALA PHE GLU ALA GLN LEU ALA GLN HIS ALA GLY GLU LEU
SEQRES 19 B 457 ALA ALA VAL VAL VAL GLU PRO VAL VAL GLN GLY ALA GLY
SEQRES 20 B 457 GLY MET ARG PHE HIS ASP PRO ARG TYR LEU HIS ASP LEU
SEQRES 21 B 457 ARG ASP ILE CYS ARG ARG TYR GLU VAL LEU LEU ILE PHE
SEQRES 22 B 457 ASP GLU ILE ALA THR GLY PHE GLY ARG THR GLY ALA LEU
SEQRES 23 B 457 PHE ALA ALA ASP HIS ALA GLY VAL SER PRO ASP ILE MET
SEQRES 24 B 457 CYS VAL GLY LYS ALA LEU THR GLY GLY TYR LEU SER LEU
SEQRES 25 B 457 ALA ALA THR LEU CYS THR ALA ASP VAL ALA HIS THR ILE
SEQRES 26 B 457 SER ALA GLY ALA ALA GLY ALA LEU MET HIS GLY PRO THR
SEQRES 27 B 457 PHE MET ALA ASN PRO LEU ALA CYS ALA VAL SER VAL ALA
SEQRES 28 B 457 SER VAL GLU LEU LEU LEU GLY GLN ASP TRP ARG THR ARG
SEQRES 29 B 457 ILE THR GLU LEU ALA ALA GLY LEU THR ALA GLY LEU ASP
SEQRES 30 B 457 THR ALA ARG ALA LEU PRO ALA VAL THR ASP VAL ARG VAL
SEQRES 31 B 457 CYS GLY ALA ILE GLY VAL ILE GLU CYS ASP ARG PRO VAL
SEQRES 32 B 457 ASP LEU ALA VAL ALA THR PRO ALA ALA LEU ASP ARG GLY
SEQRES 33 B 457 VAL TRP LEU ARG PRO PHE ARG ASN LEU VAL TYR ALA MET
SEQRES 34 B 457 PRO PRO TYR ILE CYS THR PRO ALA GLU ILE THR GLN ILE
SEQRES 35 B 457 THR SER ALA MET VAL GLU VAL ALA ARG LEU VAL GLY SER
SEQRES 36 B 457 LEU PRO
HET PLP A 501 15
HET 6SQ B 501 24
HET PLP B 502 15
HETNAM PLP PYRIDOXAL-5'-PHOSPHATE
HETNAM 6SQ 1-[4-[4-(3-CHLOROPHENYL)CARBONYLPIPERIDIN-1-
HETNAM 2 6SQ YL]PHENYL]ETHANONE
HETSYN PLP VITAMIN B6 PHOSPHATE
FORMUL 3 PLP 2(C8 H10 N O6 P)
FORMUL 4 6SQ C20 H20 CL N O2
FORMUL 6 HOH *271(H2 O)
HELIX 1 AA1 THR A 9 LEU A 21 1 13
HELIX 2 AA2 MET A 61 THR A 66 1 6
HELIX 3 AA3 HIS A 73 MET A 87 1 15
HELIX 4 AA4 HIS A 97 THR A 111 1 15
HELIX 5 AA5 SER A 123 ARG A 142 1 20
HELIX 6 AA6 THR A 161 SER A 166 1 6
HELIX 7 AA7 MET A 174 THR A 179 5 6
HELIX 8 AA8 ASP A 196 GLN A 209 1 14
HELIX 9 AA9 HIS A 210 GLY A 212 5 3
HELIX 10 AB1 PRO A 234 GLU A 248 1 15
HELIX 11 AB2 PHE A 267 ALA A 272 5 6
HELIX 12 AB3 GLY A 282 GLY A 287 5 6
HELIX 13 AB4 ALA A 299 GLY A 308 1 10
HELIX 14 AB5 ASN A 322 GLY A 338 1 17
HELIX 15 AB6 ASP A 340 ASP A 357 1 18
HELIX 16 AB7 THR A 358 LEU A 362 5 5
HELIX 17 AB8 ASP A 384 ARG A 395 1 12
HELIX 18 AB9 THR A 415 GLY A 434 1 20
HELIX 19 AC1 THR B 9 LEU B 21 1 13
HELIX 20 AC2 MET B 61 THR B 66 1 6
HELIX 21 AC3 HIS B 73 MET B 87 1 15
HELIX 22 AC4 HIS B 97 THR B 111 1 15
HELIX 23 AC5 SER B 123 GLY B 141 1 19
HELIX 24 AC6 THR B 161 SER B 166 1 6
HELIX 25 AC7 MET B 174 THR B 179 5 6
HELIX 26 AC8 ASP B 196 ALA B 211 1 16
HELIX 27 AC9 PRO B 234 GLU B 248 1 15
HELIX 28 AD1 PHE B 267 ALA B 272 5 6
HELIX 29 AD2 ALA B 299 ALA B 307 1 9
HELIX 30 AD3 ASN B 322 GLY B 338 1 17
HELIX 31 AD4 ASP B 340 ASP B 357 1 18
HELIX 32 AD5 THR B 358 LEU B 362 5 5
HELIX 33 AD6 ASP B 384 ARG B 395 1 12
HELIX 34 AD7 THR B 415 SER B 435 1 21
SHEET 1 AA1 5 VAL A 397 TRP A 398 0
SHEET 2 AA1 5 GLN A 53 ASP A 59 1 N LEU A 58 O TRP A 398
SHEET 3 AA1 5 TRP A 45 ARG A 50 -1 N ARG A 50 O GLN A 53
SHEET 4 AA1 5 VAL A 36 HIS A 42 -1 N VAL A 39 O THR A 47
SHEET 5 AA1 5 LEU B 95 THR B 96 1 O THR B 96 N ALA A 38
SHEET 1 AA2 5 LEU A 95 THR A 96 0
SHEET 2 AA2 5 VAL B 36 HIS B 42 1 O ALA B 38 N THR A 96
SHEET 3 AA2 5 TRP B 45 ARG B 50 -1 O TRP B 45 N HIS B 42
SHEET 4 AA2 5 GLN B 53 ASP B 59 -1 O VAL B 57 N LEU B 46
SHEET 5 AA2 5 VAL B 397 TRP B 398 1 O TRP B 398 N LEU B 58
SHEET 1 AA3 7 LEU A 115 SER A 121 0
SHEET 2 AA3 7 ALA A 293 THR A 298 -1 O THR A 295 N PHE A 119
SHEET 3 AA3 7 ILE A 278 VAL A 281 -1 N MET A 279 O LEU A 296
SHEET 4 AA3 7 LEU A 250 ASP A 254 1 N PHE A 253 O CYS A 280
SHEET 5 AA3 7 LEU A 214 VAL A 219 1 N VAL A 217 O ILE A 252
SHEET 6 AA3 7 ARG A 149 TRP A 153 1 N ARG A 149 O ALA A 215
SHEET 7 AA3 7 VAL A 186 ALA A 188 1 O ALA A 188 N THR A 152
SHEET 1 AA4 2 VAL A 223 GLN A 224 0
SHEET 2 AA4 2 ARG A 230 PHE A 231 -1 O ARG A 230 N GLN A 224
SHEET 1 AA5 3 VAL A 365 VAL A 370 0
SHEET 2 AA5 3 GLY A 375 CYS A 379 -1 O GLU A 378 N THR A 366
SHEET 3 AA5 3 LEU A 405 ALA A 408 -1 O VAL A 406 N ILE A 377
SHEET 1 AA6 7 LEU B 115 SER B 121 0
SHEET 2 AA6 7 ALA B 293 THR B 298 -1 O THR B 295 N PHE B 119
SHEET 3 AA6 7 ILE B 278 VAL B 281 -1 N MET B 279 O LEU B 296
SHEET 4 AA6 7 LEU B 250 ASP B 254 1 N PHE B 253 O ILE B 278
SHEET 5 AA6 7 LEU B 214 VAL B 219 1 N VAL B 217 O ILE B 252
SHEET 6 AA6 7 ARG B 149 TRP B 153 1 N ARG B 149 O ALA B 215
SHEET 7 AA6 7 VAL B 186 ALA B 188 1 O ALA B 188 N THR B 152
SHEET 1 AA7 2 VAL B 223 GLN B 224 0
SHEET 2 AA7 2 ARG B 230 PHE B 231 -1 O ARG B 230 N GLN B 224
SHEET 1 AA8 3 VAL B 365 VAL B 370 0
SHEET 2 AA8 3 GLY B 375 CYS B 379 -1 O GLU B 378 N ASP B 367
SHEET 3 AA8 3 LEU B 405 ALA B 408 -1 O VAL B 406 N ILE B 377
LINK NZ LYS A 283 C4A PLP A 501 1555 1555 1.27
LINK NZ LYS B 283 C4A PLP B 502 1555 1555 1.28
SITE 1 AC1 18 SER A 123 GLY A 124 SER A 125 TYR A 157
SITE 2 AC1 18 HIS A 158 GLY A 159 GLU A 220 ASP A 254
SITE 3 AC1 18 ILE A 256 ALA A 257 LYS A 283 HOH A 629
SITE 4 AC1 18 HOH A 665 HOH A 681 HOH A 688 HOH A 694
SITE 5 AC1 18 PRO B 317 THR B 318
SITE 1 AC2 14 MET A 91 PHE A 92 GLY A 93 GLY A 316
SITE 2 AC2 14 THR A 318 TYR B 25 TRP B 64 GLY B 156
SITE 3 AC2 14 TYR B 157 ASP B 169 GLY B 172 GLY B 173
SITE 4 AC2 14 ALA B 226 ARG B 403
SITE 1 AC3 19 THR A 318 HOH A 626 TRP B 64 TRP B 65
SITE 2 AC3 19 THR B 66 SER B 123 GLY B 124 SER B 125
SITE 3 AC3 19 TYR B 157 HIS B 158 GLU B 220 ASP B 254
SITE 4 AC3 19 ILE B 256 ALA B 257 GLY B 282 ALA B 284
SITE 5 AC3 19 LEU B 285 HOH B 662 HOH B 680
CRYST1 63.024 66.085 202.147 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 0.015867 0.000000 0.000000 0.00000
SCALE2 0.000000 0.015132 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004947 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
