HEADER OXIDOREDUCTASE/ANTIBIOTIC 31-JAN-14 4OOF
TITLE M. TUBERCULOSIS 1-DEOXY-D-XYLULOSE-5-PHOSPHATE REDUCTOISOMERASE W203F
TITLE 2 MUTANT BOUND TO FOSMIDOMYCIN AND NADPH
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: 1-DEOXY-D-XYLULOSE 5-PHOSPHATE REDUCTOISOMERASE;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: UNP RESIDUES 1-389;
COMPND 5 SYNONYM: DXP REDUCTOISOMERASE, 1-DEOXYXYLULOSE-5-PHOSPHATE
COMPND 6 REDUCTOISOMERASE, 2-C-METHYL-D-ERYTHRITOL 4-PHOSPHATE SYNTHASE;
COMPND 7 EC: 1.1.1.267;
COMPND 8 ENGINEERED: YES;
COMPND 9 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MYCOBACTERIUM TUBERCULOSIS;
SOURCE 3 ORGANISM_TAXID: 83332;
SOURCE 4 STRAIN: HRV37;
SOURCE 5 GENE: DXR, RVBD_2870C;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS REDUCTOISOMERASE, OXIDOREDUCTASE-ANTIBIOTIC COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR C.L.ALLEN,S.A.KHOLODAR,A.S.MURKIN,A.M.GULICK
REVDAT 2 20-SEP-23 4OOF 1 REMARK SEQADV LINK
REVDAT 1 18-JUN-14 4OOF 0
JRNL AUTH S.A.KHOLODAR,G.TOMBLINE,J.LIU,Z.TAN,C.L.ALLEN,A.M.GULICK,
JRNL AUTH 2 A.S.MURKIN
JRNL TITL ALTERATION OF THE FLEXIBLE LOOP IN
JRNL TITL 2 1-DEOXY-D-XYLULOSE-5-PHOSPHATE REDUCTOISOMERASE BOOSTS
JRNL TITL 3 ENTHALPY-DRIVEN INHIBITION BY FOSMIDOMYCIN.
JRNL REF BIOCHEMISTRY V. 53 3423 2014
JRNL REFN ISSN 0006-2960
JRNL PMID 24825256
JRNL DOI 10.1021/BI5004074
REMARK 2
REMARK 2 RESOLUTION. 2.30 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.8.1_1168)
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) : 2.30
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 34.78
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 36380
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.162
REMARK 3 R VALUE (WORKING SET) : 0.159
REMARK 3 FREE R VALUE : 0.212
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.010
REMARK 3 FREE R VALUE TEST SET COUNT : 1821
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 34.7861 - 5.4028 1.00 2875 135 0.1405 0.1551
REMARK 3 2 5.4028 - 4.2909 1.00 2743 129 0.1315 0.1734
REMARK 3 3 4.2909 - 3.7492 1.00 2703 127 0.1400 0.1787
REMARK 3 4 3.7492 - 3.4068 1.00 2643 154 0.1624 0.2083
REMARK 3 5 3.4068 - 3.1628 1.00 2661 129 0.1781 0.2349
REMARK 3 6 3.1628 - 2.9764 1.00 2654 141 0.1800 0.2422
REMARK 3 7 2.9764 - 2.8274 1.00 2611 165 0.1802 0.2493
REMARK 3 8 2.8274 - 2.7044 1.00 2634 137 0.1752 0.2555
REMARK 3 9 2.7044 - 2.6003 1.00 2613 140 0.1763 0.2508
REMARK 3 10 2.6003 - 2.5106 1.00 2616 132 0.1725 0.2572
REMARK 3 11 2.5106 - 2.4321 1.00 2635 134 0.1815 0.2484
REMARK 3 12 2.4321 - 2.3626 1.00 2603 151 0.1794 0.2405
REMARK 3 13 2.3626 - 2.3000 1.00 2568 147 0.2003 0.2720
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) : 0.220
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 20.360
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 32.70
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
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 : 0.007 5703
REMARK 3 ANGLE : 1.136 7814
REMARK 3 CHIRALITY : 0.066 924
REMARK 3 PLANARITY : 0.005 1019
REMARK 3 DIHEDRAL : 15.962 1998
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 4OOF COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 04-FEB-14.
REMARK 100 THE DEPOSITION ID IS D_1000084748.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 12-AUG-12
REMARK 200 TEMPERATURE (KELVIN) : 113
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRL
REMARK 200 BEAMLINE : BL7-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.127
REMARK 200 MONOCHROMATOR : SIDE SCATTERING I-BEAM BENT
REMARK 200 SINGLE CRYSTAL, ASYMMETRIC CUT
REMARK 200 4.9650 DEGREES
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 36447
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.300
REMARK 200 RESOLUTION RANGE LOW (A) : 84.639
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : 0.09200
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 9.9000
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) : 2.40
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.48800
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.700
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: PDB ENTRY 4A03
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 47.64
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.35
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 30% PEG8000, 50 MM MES, 200 MM
REMARK 280 AMMONIUM ACETATE, PH 6.5, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 293K
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 68.21900
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 53.95600
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 53.95600
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 102.32850
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 53.95600
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 53.95600
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 34.10950
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 53.95600
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 53.95600
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 102.32850
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 53.95600
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 53.95600
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 34.10950
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 68.21900
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: 7340 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 26550 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -49.0 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 -13
REMARK 465 HIS A -12
REMARK 465 HIS A -11
REMARK 465 HIS A -10
REMARK 465 HIS A -9
REMARK 465 HIS A -8
REMARK 465 HIS 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 THR A 2
REMARK 465 ASN A 3
REMARK 465 SER A 4
REMARK 465 THR A 5
REMARK 465 ASP A 6
REMARK 465 GLY A 7
REMARK 465 ARG A 8
REMARK 465 ALA A 9
REMARK 465 ASP A 10
REMARK 465 MET A 389
REMARK 465 MET B -13
REMARK 465 HIS B -12
REMARK 465 HIS B -11
REMARK 465 HIS B -10
REMARK 465 HIS B -9
REMARK 465 HIS B -8
REMARK 465 HIS 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 THR B 2
REMARK 465 ASN B 3
REMARK 465 SER B 4
REMARK 465 THR B 5
REMARK 465 ASP B 6
REMARK 465 GLY B 7
REMARK 465 ARG B 8
REMARK 465 ALA B 9
REMARK 465 ASP B 10
REMARK 465 MET B 389
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 ASP A 37 CG OD1 OD2
REMARK 470 GLN A 75 CD OE1 NE2
REMARK 470 LYS A 118 CE NZ
REMARK 470 ARG A 140 CD NE CZ NH1 NH2
REMARK 470 ARG A 143 NE CZ NH1 NH2
REMARK 470 GLU A 195 CG CD OE1 OE2
REMARK 470 ARG A 279 CG CD NE CZ NH1 NH2
REMARK 470 HIS A 356 CG ND1 CD2 CE1 NE2
REMARK 470 ASP B 37 CG OD1 OD2
REMARK 470 LEU B 51 CG CD1 CD2
REMARK 470 HIS B 72 CG ND1 CD2 CE1 NE2
REMARK 470 ARG B 76 CG CD NE CZ NH1 NH2
REMARK 470 VAL B 77 CG1 CG2
REMARK 470 ASP B 79 CG OD1 OD2
REMARK 470 LYS B 118 CE NZ
REMARK 470 LYS B 171 NZ
REMARK 470 GLU B 195 CG CD OE1 OE2
REMARK 470 GLU B 380 CG CD OE1 OE2
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 ASN A 65 84.69 -68.61
REMARK 500 SER A 249 173.29 168.76
REMARK 500 ASP A 266 106.24 -172.38
REMARK 500 PHE A 306 79.86 -119.14
REMARK 500 ALA A 362 41.36 -81.32
REMARK 500 SER B 249 173.30 165.17
REMARK 500 ASP B 266 105.36 -171.13
REMARK 500 ALA B 362 22.55 -77.53
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 MN A 401 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 151 OD1
REMARK 620 2 GLU A 153 OE1 100.8
REMARK 620 3 GLU A 222 OE2 98.9 101.1
REMARK 620 4 FOM A 402 O2 111.8 145.1 86.3
REMARK 620 5 FOM A 402 O1 89.2 94.7 160.5 74.3
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MN B 401 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 151 OD1
REMARK 620 2 GLU B 153 OE1 98.6
REMARK 620 3 GLU B 222 OE2 104.3 96.0
REMARK 620 4 FOM B 402 O2 117.2 142.5 86.4
REMARK 620 5 FOM B 402 O1 87.6 95.9 161.8 75.8
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 NDP A 400
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FOM A 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NDP B 400
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN B 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FOM B 402
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3ZHX RELATED DB: PDB
REMARK 900 DXR
REMARK 900 RELATED ID: 4AIC RELATED DB: PDB
REMARK 900 DXR
REMARK 900 RELATED ID: 4OOE RELATED DB: PDB
DBREF 4OOF A 1 389 UNP I6YAH0 I6YAH0_MYCTU 1 389
DBREF 4OOF B 1 389 UNP I6YAH0 I6YAH0_MYCTU 1 389
SEQADV 4OOF MET A -13 UNP I6YAH0 EXPRESSION TAG
SEQADV 4OOF HIS A -12 UNP I6YAH0 EXPRESSION TAG
SEQADV 4OOF HIS A -11 UNP I6YAH0 EXPRESSION TAG
SEQADV 4OOF HIS A -10 UNP I6YAH0 EXPRESSION TAG
SEQADV 4OOF HIS A -9 UNP I6YAH0 EXPRESSION TAG
SEQADV 4OOF HIS A -8 UNP I6YAH0 EXPRESSION TAG
SEQADV 4OOF HIS A -7 UNP I6YAH0 EXPRESSION TAG
SEQADV 4OOF LEU A -6 UNP I6YAH0 EXPRESSION TAG
SEQADV 4OOF VAL A -5 UNP I6YAH0 EXPRESSION TAG
SEQADV 4OOF PRO A -4 UNP I6YAH0 EXPRESSION TAG
SEQADV 4OOF ARG A -3 UNP I6YAH0 EXPRESSION TAG
SEQADV 4OOF GLY A -2 UNP I6YAH0 EXPRESSION TAG
SEQADV 4OOF SER A -1 UNP I6YAH0 EXPRESSION TAG
SEQADV 4OOF HIS A 0 UNP I6YAH0 EXPRESSION TAG
SEQADV 4OOF PHE A 203 UNP I6YAH0 TRP 203 ENGINEERED MUTATION
SEQADV 4OOF MET B -13 UNP I6YAH0 EXPRESSION TAG
SEQADV 4OOF HIS B -12 UNP I6YAH0 EXPRESSION TAG
SEQADV 4OOF HIS B -11 UNP I6YAH0 EXPRESSION TAG
SEQADV 4OOF HIS B -10 UNP I6YAH0 EXPRESSION TAG
SEQADV 4OOF HIS B -9 UNP I6YAH0 EXPRESSION TAG
SEQADV 4OOF HIS B -8 UNP I6YAH0 EXPRESSION TAG
SEQADV 4OOF HIS B -7 UNP I6YAH0 EXPRESSION TAG
SEQADV 4OOF LEU B -6 UNP I6YAH0 EXPRESSION TAG
SEQADV 4OOF VAL B -5 UNP I6YAH0 EXPRESSION TAG
SEQADV 4OOF PRO B -4 UNP I6YAH0 EXPRESSION TAG
SEQADV 4OOF ARG B -3 UNP I6YAH0 EXPRESSION TAG
SEQADV 4OOF GLY B -2 UNP I6YAH0 EXPRESSION TAG
SEQADV 4OOF SER B -1 UNP I6YAH0 EXPRESSION TAG
SEQADV 4OOF HIS B 0 UNP I6YAH0 EXPRESSION TAG
SEQADV 4OOF PHE B 203 UNP I6YAH0 TRP 203 ENGINEERED MUTATION
SEQRES 1 A 403 MET HIS HIS HIS HIS HIS HIS LEU VAL PRO ARG GLY SER
SEQRES 2 A 403 HIS MET THR ASN SER THR ASP GLY ARG ALA ASP GLY ARG
SEQRES 3 A 403 LEU ARG VAL VAL VAL LEU GLY SER THR GLY SER ILE GLY
SEQRES 4 A 403 THR GLN ALA LEU GLN VAL ILE ALA ASP ASN PRO ASP ARG
SEQRES 5 A 403 PHE GLU VAL VAL GLY LEU ALA ALA GLY GLY ALA HIS LEU
SEQRES 6 A 403 ASP THR LEU LEU ARG GLN ARG ALA GLN THR GLY VAL THR
SEQRES 7 A 403 ASN ILE ALA VAL ALA ASP GLU HIS ALA ALA GLN ARG VAL
SEQRES 8 A 403 GLY ASP ILE PRO TYR HIS GLY SER ASP ALA ALA THR ARG
SEQRES 9 A 403 LEU VAL GLU GLN THR GLU ALA ASP VAL VAL LEU ASN ALA
SEQRES 10 A 403 LEU VAL GLY ALA LEU GLY LEU ARG PRO THR LEU ALA ALA
SEQRES 11 A 403 LEU LYS THR GLY ALA ARG LEU ALA LEU ALA ASN LYS GLU
SEQRES 12 A 403 SER LEU VAL ALA GLY GLY SER LEU VAL LEU ARG ALA ALA
SEQRES 13 A 403 ARG PRO GLY GLN ILE VAL PRO VAL ASP SER GLU HIS SER
SEQRES 14 A 403 ALA LEU ALA GLN CYS LEU ARG GLY GLY THR PRO ASP GLU
SEQRES 15 A 403 VAL ALA LYS LEU VAL LEU THR ALA SER GLY GLY PRO PHE
SEQRES 16 A 403 ARG GLY TRP SER ALA ALA ASP LEU GLU HIS VAL THR PRO
SEQRES 17 A 403 GLU GLN ALA GLY ALA HIS PRO THR PHE SER MET GLY PRO
SEQRES 18 A 403 MET ASN THR LEU ASN SER ALA SER LEU VAL ASN LYS GLY
SEQRES 19 A 403 LEU GLU VAL ILE GLU THR HIS LEU LEU PHE GLY ILE PRO
SEQRES 20 A 403 TYR ASP ARG ILE ASP VAL VAL VAL HIS PRO GLN SER ILE
SEQRES 21 A 403 ILE HIS SER MET VAL THR PHE ILE ASP GLY SER THR ILE
SEQRES 22 A 403 ALA GLN ALA SER PRO PRO ASP MET LYS LEU PRO ILE SER
SEQRES 23 A 403 LEU ALA LEU GLY TRP PRO ARG ARG VAL SER GLY ALA ALA
SEQRES 24 A 403 ALA ALA CYS ASP PHE HIS THR ALA SER SER TRP GLU PHE
SEQRES 25 A 403 GLU PRO LEU ASP THR ASP VAL PHE PRO ALA VAL GLU LEU
SEQRES 26 A 403 ALA ARG GLN ALA GLY VAL ALA GLY GLY CYS MET THR ALA
SEQRES 27 A 403 VAL TYR ASN ALA ALA ASN GLU GLU ALA ALA ALA ALA PHE
SEQRES 28 A 403 LEU ALA GLY ARG ILE GLY PHE PRO ALA ILE VAL GLY ILE
SEQRES 29 A 403 ILE ALA ASP VAL LEU HIS ALA ALA ASP GLN TRP ALA VAL
SEQRES 30 A 403 GLU PRO ALA THR VAL ASP ASP VAL LEU ASP ALA GLN ARG
SEQRES 31 A 403 TRP ALA ARG GLU ARG ALA GLN ARG ALA VAL SER GLY MET
SEQRES 1 B 403 MET HIS HIS HIS HIS HIS HIS LEU VAL PRO ARG GLY SER
SEQRES 2 B 403 HIS MET THR ASN SER THR ASP GLY ARG ALA ASP GLY ARG
SEQRES 3 B 403 LEU ARG VAL VAL VAL LEU GLY SER THR GLY SER ILE GLY
SEQRES 4 B 403 THR GLN ALA LEU GLN VAL ILE ALA ASP ASN PRO ASP ARG
SEQRES 5 B 403 PHE GLU VAL VAL GLY LEU ALA ALA GLY GLY ALA HIS LEU
SEQRES 6 B 403 ASP THR LEU LEU ARG GLN ARG ALA GLN THR GLY VAL THR
SEQRES 7 B 403 ASN ILE ALA VAL ALA ASP GLU HIS ALA ALA GLN ARG VAL
SEQRES 8 B 403 GLY ASP ILE PRO TYR HIS GLY SER ASP ALA ALA THR ARG
SEQRES 9 B 403 LEU VAL GLU GLN THR GLU ALA ASP VAL VAL LEU ASN ALA
SEQRES 10 B 403 LEU VAL GLY ALA LEU GLY LEU ARG PRO THR LEU ALA ALA
SEQRES 11 B 403 LEU LYS THR GLY ALA ARG LEU ALA LEU ALA ASN LYS GLU
SEQRES 12 B 403 SER LEU VAL ALA GLY GLY SER LEU VAL LEU ARG ALA ALA
SEQRES 13 B 403 ARG PRO GLY GLN ILE VAL PRO VAL ASP SER GLU HIS SER
SEQRES 14 B 403 ALA LEU ALA GLN CYS LEU ARG GLY GLY THR PRO ASP GLU
SEQRES 15 B 403 VAL ALA LYS LEU VAL LEU THR ALA SER GLY GLY PRO PHE
SEQRES 16 B 403 ARG GLY TRP SER ALA ALA ASP LEU GLU HIS VAL THR PRO
SEQRES 17 B 403 GLU GLN ALA GLY ALA HIS PRO THR PHE SER MET GLY PRO
SEQRES 18 B 403 MET ASN THR LEU ASN SER ALA SER LEU VAL ASN LYS GLY
SEQRES 19 B 403 LEU GLU VAL ILE GLU THR HIS LEU LEU PHE GLY ILE PRO
SEQRES 20 B 403 TYR ASP ARG ILE ASP VAL VAL VAL HIS PRO GLN SER ILE
SEQRES 21 B 403 ILE HIS SER MET VAL THR PHE ILE ASP GLY SER THR ILE
SEQRES 22 B 403 ALA GLN ALA SER PRO PRO ASP MET LYS LEU PRO ILE SER
SEQRES 23 B 403 LEU ALA LEU GLY TRP PRO ARG ARG VAL SER GLY ALA ALA
SEQRES 24 B 403 ALA ALA CYS ASP PHE HIS THR ALA SER SER TRP GLU PHE
SEQRES 25 B 403 GLU PRO LEU ASP THR ASP VAL PHE PRO ALA VAL GLU LEU
SEQRES 26 B 403 ALA ARG GLN ALA GLY VAL ALA GLY GLY CYS MET THR ALA
SEQRES 27 B 403 VAL TYR ASN ALA ALA ASN GLU GLU ALA ALA ALA ALA PHE
SEQRES 28 B 403 LEU ALA GLY ARG ILE GLY PHE PRO ALA ILE VAL GLY ILE
SEQRES 29 B 403 ILE ALA ASP VAL LEU HIS ALA ALA ASP GLN TRP ALA VAL
SEQRES 30 B 403 GLU PRO ALA THR VAL ASP ASP VAL LEU ASP ALA GLN ARG
SEQRES 31 B 403 TRP ALA ARG GLU ARG ALA GLN ARG ALA VAL SER GLY MET
HET NDP A 400 48
HET MN A 401 1
HET FOM A 402 11
HET NDP B 400 48
HET MN B 401 1
HET FOM B 402 11
HETNAM NDP NADPH DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE
HETNAM 2 NDP PHOSPHATE
HETNAM MN MANGANESE (II) ION
HETNAM FOM 3-[FORMYL(HYDROXY)AMINO]PROPYLPHOSPHONIC ACID
HETSYN FOM FOSMIDOMYCIN
FORMUL 3 NDP 2(C21 H30 N7 O17 P3)
FORMUL 4 MN 2(MN 2+)
FORMUL 5 FOM 2(C4 H10 N O5 P)
FORMUL 9 HOH *394(H2 O)
HELIX 1 1 GLY A 22 ASP A 34 1 13
HELIX 2 2 HIS A 50 GLY A 62 1 13
HELIX 3 3 ASP A 70 GLY A 78 1 9
HELIX 4 4 ASP A 86 GLN A 94 1 9
HELIX 5 5 GLY A 106 LEU A 108 5 3
HELIX 6 6 GLY A 109 GLY A 120 1 12
HELIX 7 7 ASN A 127 GLY A 135 1 9
HELIX 8 8 GLY A 135 ALA A 142 1 8
HELIX 9 9 ASP A 151 ARG A 162 1 12
HELIX 10 10 GLY A 163 GLY A 164 5 2
HELIX 11 11 THR A 165 ASP A 167 5 3
HELIX 12 12 SER A 185 HIS A 191 1 7
HELIX 13 13 THR A 193 GLY A 198 1 6
HELIX 14 14 GLY A 206 LEU A 216 1 11
HELIX 15 15 LEU A 216 GLY A 231 1 16
HELIX 16 16 PRO A 233 ASP A 235 5 3
HELIX 17 17 MET A 267 TRP A 277 1 11
HELIX 18 18 PRO A 307 GLY A 319 1 13
HELIX 19 19 CYS A 321 ALA A 339 1 19
HELIX 20 20 PRO A 345 ALA A 357 1 13
HELIX 21 21 ALA A 358 ALA A 362 5 5
HELIX 22 22 THR A 367 SER A 387 1 21
HELIX 23 23 GLY B 22 ASN B 35 1 14
HELIX 24 24 HIS B 50 GLY B 62 1 13
HELIX 25 25 ASP B 70 GLY B 78 1 9
HELIX 26 26 ASP B 86 THR B 95 1 10
HELIX 27 27 GLY B 106 LEU B 108 5 3
HELIX 28 28 GLY B 109 THR B 119 1 11
HELIX 29 29 ASN B 127 GLY B 135 1 9
HELIX 30 30 GLY B 135 ALA B 141 1 7
HELIX 31 31 ASP B 151 LEU B 161 1 11
HELIX 32 32 ARG B 162 GLY B 164 5 3
HELIX 33 33 THR B 165 ASP B 167 5 3
HELIX 34 34 SER B 185 GLU B 190 1 6
HELIX 35 35 THR B 193 GLY B 198 1 6
HELIX 36 36 GLY B 206 LEU B 216 1 11
HELIX 37 37 LEU B 216 GLY B 231 1 16
HELIX 38 38 PRO B 233 ASP B 235 5 3
HELIX 39 39 MET B 267 TRP B 277 1 11
HELIX 40 40 PRO B 307 GLY B 319 1 13
HELIX 41 41 CYS B 321 ALA B 339 1 19
HELIX 42 42 PRO B 345 HIS B 356 1 12
HELIX 43 43 ALA B 357 ALA B 362 5 6
HELIX 44 44 THR B 367 GLY B 388 1 22
SHEET 1 A 7 TYR A 82 HIS A 83 0
SHEET 2 A 7 ILE A 66 VAL A 68 1 N VAL A 68 O TYR A 82
SHEET 3 A 7 PHE A 39 ALA A 46 1 N LEU A 44 O ALA A 67
SHEET 4 A 7 LEU A 13 LEU A 18 1 N VAL A 15 O GLU A 40
SHEET 5 A 7 VAL A 99 ASN A 102 1 O LEU A 101 N VAL A 16
SHEET 6 A 7 ARG A 122 LEU A 125 1 O ARG A 122 N VAL A 100
SHEET 7 A 7 ILE A 147 PRO A 149 1 O VAL A 148 N LEU A 123
SHEET 1 B 8 ILE A 237 VAL A 241 0
SHEET 2 B 8 VAL A 169 ALA A 176 1 N LEU A 174 O ASP A 238
SHEET 3 B 8 ILE A 247 PHE A 253 -1 O MET A 250 N VAL A 173
SHEET 4 B 8 THR A 258 ALA A 262 -1 O ILE A 259 N VAL A 251
SHEET 5 B 8 THR B 258 ALA B 262 -1 O THR B 258 N ALA A 262
SHEET 6 B 8 ILE B 247 PHE B 253 -1 N VAL B 251 O ILE B 259
SHEET 7 B 8 VAL B 169 ALA B 176 -1 N VAL B 173 O MET B 250
SHEET 8 B 8 ILE B 237 VAL B 241 1 O ASP B 238 N LEU B 172
SHEET 1 C 2 SER A 294 PHE A 298 0
SHEET 2 C 2 SER B 294 PHE B 298 -1 O TRP B 296 N TRP A 296
SHEET 1 D 7 TYR B 82 HIS B 83 0
SHEET 2 D 7 ILE B 66 VAL B 68 1 N VAL B 68 O TYR B 82
SHEET 3 D 7 PHE B 39 ALA B 46 1 N LEU B 44 O ALA B 67
SHEET 4 D 7 LEU B 13 LEU B 18 1 N VAL B 15 O GLU B 40
SHEET 5 D 7 VAL B 99 ASN B 102 1 O LEU B 101 N VAL B 16
SHEET 6 D 7 ARG B 122 LEU B 125 1 O ARG B 122 N VAL B 100
SHEET 7 D 7 ILE B 147 PRO B 149 1 O VAL B 148 N LEU B 123
LINK OD1 ASP A 151 MN MN A 401 1555 1555 2.06
LINK OE1 GLU A 153 MN MN A 401 1555 1555 2.01
LINK OE2 GLU A 222 MN MN A 401 1555 1555 2.10
LINK MN MN A 401 O2 FOM A 402 1555 1555 1.97
LINK MN MN A 401 O1 FOM A 402 1555 1555 2.23
LINK OD1 ASP B 151 MN MN B 401 1555 1555 1.97
LINK OE1 GLU B 153 MN MN B 401 1555 1555 2.08
LINK OE2 GLU B 222 MN MN B 401 1555 1555 2.02
LINK MN MN B 401 O2 FOM B 402 1555 1555 2.01
LINK MN MN B 401 O1 FOM B 402 1555 1555 2.18
CISPEP 1 TRP A 277 PRO A 278 0 4.57
CISPEP 2 TRP B 277 PRO B 278 0 4.78
SITE 1 AC1 35 GLY A 19 THR A 21 GLY A 22 SER A 23
SITE 2 AC1 35 ILE A 24 ALA A 46 GLY A 47 GLY A 48
SITE 3 AC1 35 ALA A 49 HIS A 50 ALA A 69 ALA A 103
SITE 4 AC1 35 LEU A 104 VAL A 105 LEU A 108 ALA A 126
SITE 5 AC1 35 ASN A 127 LYS A 128 GLU A 129 ASP A 151
SITE 6 AC1 35 MET A 205 GLY A 206 PRO A 207 ASN A 209
SITE 7 AC1 35 MET A 267 FOM A 402 HOH A 501 HOH A 511
SITE 8 AC1 35 HOH A 532 HOH A 541 HOH A 560 HOH A 579
SITE 9 AC1 35 HOH A 583 HOH A 621 HOH A 636
SITE 1 AC2 5 LYS A 128 ASP A 151 GLU A 153 GLU A 222
SITE 2 AC2 5 FOM A 402
SITE 1 AC3 18 LYS A 128 ASP A 151 SER A 152 GLU A 153
SITE 2 AC3 18 ALA A 176 SER A 177 HIS A 200 PHE A 203
SITE 3 AC3 18 MET A 205 SER A 213 ASN A 218 LYS A 219
SITE 4 AC3 18 GLU A 222 NDP A 400 MN A 401 HOH A 506
SITE 5 AC3 18 HOH A 509 HOH A 530
SITE 1 AC4 34 GLY B 19 THR B 21 GLY B 22 SER B 23
SITE 2 AC4 34 ILE B 24 ALA B 46 GLY B 47 GLY B 48
SITE 3 AC4 34 ALA B 49 HIS B 50 ALA B 69 ALA B 103
SITE 4 AC4 34 LEU B 104 VAL B 105 LEU B 108 ALA B 126
SITE 5 AC4 34 ASN B 127 LYS B 128 GLU B 129 ASP B 151
SITE 6 AC4 34 MET B 205 GLY B 206 ASN B 209 MET B 267
SITE 7 AC4 34 FOM B 402 HOH B 504 HOH B 506 HOH B 531
SITE 8 AC4 34 HOH B 565 HOH B 570 HOH B 600 HOH B 640
SITE 9 AC4 34 HOH B 656 HOH B 663
SITE 1 AC5 4 ASP B 151 GLU B 153 GLU B 222 FOM B 402
SITE 1 AC6 17 ASP B 151 SER B 152 GLU B 153 ALA B 176
SITE 2 AC6 17 SER B 177 HIS B 200 PHE B 203 MET B 205
SITE 3 AC6 17 SER B 213 ASN B 218 LYS B 219 GLU B 222
SITE 4 AC6 17 NDP B 400 MN B 401 HOH B 503 HOH B 514
SITE 5 AC6 17 HOH B 517
CRYST1 107.912 107.912 136.438 90.00 90.00 90.00 P 43 21 2 16
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 0.009267 0.000000 0.000000 0.00000
SCALE2 0.000000 0.009267 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007329 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
