HEADER TRANSFERASE/TRANSFERASE INHIBITOR 11-JUN-15 5BYT
TITLE PRPP COMPLEXED WITH A SINGLE MG IN THE ACTIVE SITE OF MYCOBACTERIUM
TITLE 2 TUBERCULOSIS ANTHRANILATE PHOSPHORIBOSYLTRANSFERASE (ANPRT; TRPD)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ANTHRANILATE PHOSPHORIBOSYLTRANSFERASE;
COMPND 3 CHAIN: A, B;
COMPND 4 EC: 2.4.2.18;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MYCOBACTERIUM TUBERCULOSIS;
SOURCE 3 ORGANISM_TAXID: 83332;
SOURCE 4 STRAIN: ATCC 25618 / H37RV;
SOURCE 5 GENE: TRPD, RV2192C, MTCY190.03C;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: C41(DE3)PLYSS;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET23A
KEYWDS PRPP, PHOSPHORIBOYSL PYROPHOSPHATE, TB STRUCTURAL GENOMICS
KEYWDS 2 CONSORTIUM, TBSGC, MAGNESIUM BINDING, TRANSFERASE-TRANSFERASE
KEYWDS 3 INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR G.L.EVANS,E.N.BAKER,J.S.LOTT,TB STRUCTURAL GENOMICS CONSORTIUM
AUTHOR 2 (TBSGC)
REVDAT 5 27-SEP-23 5BYT 1 HETSYN
REVDAT 4 29-JUL-20 5BYT 1 COMPND REMARK HETNAM LINK
REVDAT 4 2 1 SITE
REVDAT 3 01-JAN-20 5BYT 1 REMARK
REVDAT 2 20-SEP-17 5BYT 1 REMARK
REVDAT 1 20-JUL-16 5BYT 0
JRNL AUTH G.L.EVANS,E.N.BAKER,J.S.LOTT
JRNL TITL BINDING AND MIMICKING OF THE PHOSPHATE-RICH SUBSTRATE, PRPP.
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.9_1692
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) : 2.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 39.29
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 3 NUMBER OF REFLECTIONS : 49059
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.225
REMARK 3 R VALUE (WORKING SET) : 0.223
REMARK 3 FREE R VALUE : 0.271
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.030
REMARK 3 FREE R VALUE TEST SET COUNT : 2470
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 39.2966 - 4.9294 0.99 3278 185 0.1767 0.1671
REMARK 3 2 4.9294 - 3.9138 1.00 3186 166 0.1710 0.1996
REMARK 3 3 3.9138 - 3.4194 1.00 3159 138 0.1971 0.2696
REMARK 3 4 3.4194 - 3.1069 1.00 3113 172 0.2195 0.2848
REMARK 3 5 3.1069 - 2.8843 1.00 3089 186 0.2220 0.3117
REMARK 3 6 2.8843 - 2.7143 1.00 3110 155 0.2242 0.3065
REMARK 3 7 2.7143 - 2.5783 1.00 3087 169 0.2298 0.2634
REMARK 3 8 2.5783 - 2.4661 1.00 3068 170 0.2242 0.2799
REMARK 3 9 2.4661 - 2.3712 1.00 3092 170 0.2343 0.2954
REMARK 3 10 2.3712 - 2.2894 1.00 3029 195 0.2469 0.3060
REMARK 3 11 2.2894 - 2.2178 1.00 3066 166 0.3436 0.4049
REMARK 3 12 2.2178 - 2.1544 1.00 3056 167 0.2873 0.3529
REMARK 3 13 2.1544 - 2.0977 1.00 3057 162 0.2578 0.3187
REMARK 3 14 2.0977 - 2.0465 1.00 3108 136 0.2617 0.3055
REMARK 3 15 2.0465 - 2.0000 1.00 3091 133 0.2838 0.3040
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) : 0.280
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 30.340
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
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 : 0.003 5231
REMARK 3 ANGLE : 0.714 7177
REMARK 3 CHIRALITY : 0.028 828
REMARK 3 PLANARITY : 0.003 952
REMARK 3 DIHEDRAL : 11.207 1816
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 5BYT COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 11-JUN-15.
REMARK 100 THE DEPOSITION ID IS D_1000210673.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 27-MAR-15
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.0
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : AUSTRALIAN SYNCHROTRON
REMARK 200 BEAMLINE : MX1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9537
REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL SI(111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 210R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS NOVEMBER 3, 2014
REMARK 200 DATA SCALING SOFTWARE : AIMLESS 0.3.11
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 49191
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000
REMARK 200 RESOLUTION RANGE LOW (A) : 40.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 6.200
REMARK 200 R MERGE (I) : 0.17500
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 8.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.05
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 6.20
REMARK 200 R MERGE FOR SHELL (I) : 1.17600
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 2.5.6
REMARK 200 STARTING MODEL: PDB ENTRY 3QR9 CHAIN A
REMARK 200
REMARK 200 REMARK: FLAT-DIAMOND SHAPE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 46.60
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.30
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M IMIDAZOLE-MALATE, 15% PEG-4000,
REMARK 280 PH 7.0, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 291K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z
REMARK 290 3555 -X+1/2,Y+1/2,-Z
REMARK 290 4555 X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 56.00550
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 40.59600
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 56.00550
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 40.59600
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: 3270 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 25150 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -66.0 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 0
REMARK 465 VAL A 1
REMARK 465 ALA A 2
REMARK 465 LEU A 3
REMARK 465 SER A 4
REMARK 465 ALA A 5
REMARK 465 GLU A 6
REMARK 465 GLY A 7
REMARK 465 SER A 8
REMARK 465 SER A 9
REMARK 465 GLY A 10
REMARK 465 GLY A 11
REMARK 465 SER A 12
REMARK 465 ARG A 13
REMARK 465 GLY A 14
REMARK 465 GLY A 15
REMARK 465 SER A 16
REMARK 465 PRO A 17
REMARK 465 LYS A 18
REMARK 465 ALA A 19
REMARK 465 GLU A 20
REMARK 465 ALA A 21
REMARK 465 ALA A 22
REMARK 465 SER A 23
REMARK 465 SER A 332
REMARK 465 ARG A 333
REMARK 465 ALA A 334
REMARK 465 ILE A 370
REMARK 465 LEU A 371
REMARK 465 GLU A 372
REMARK 465 HIS A 373
REMARK 465 HIS A 374
REMARK 465 HIS A 375
REMARK 465 HIS A 376
REMARK 465 HIS A 377
REMARK 465 HIS A 378
REMARK 465 MET B 0
REMARK 465 VAL B 1
REMARK 465 ALA B 2
REMARK 465 LEU B 3
REMARK 465 SER B 4
REMARK 465 ALA B 5
REMARK 465 GLU B 6
REMARK 465 GLY B 7
REMARK 465 SER B 8
REMARK 465 SER B 9
REMARK 465 GLY B 10
REMARK 465 GLY B 11
REMARK 465 SER B 12
REMARK 465 ARG B 13
REMARK 465 GLY B 14
REMARK 465 GLY B 15
REMARK 465 SER B 16
REMARK 465 PRO B 17
REMARK 465 LYS B 18
REMARK 465 ALA B 19
REMARK 465 GLU B 20
REMARK 465 ALA B 21
REMARK 465 ALA B 22
REMARK 465 SER B 23
REMARK 465 SER B 332
REMARK 465 ARG B 333
REMARK 465 ALA B 334
REMARK 465 ILE B 370
REMARK 465 LEU B 371
REMARK 465 GLU B 372
REMARK 465 HIS B 373
REMARK 465 HIS B 374
REMARK 465 HIS B 375
REMARK 465 HIS B 376
REMARK 465 HIS B 377
REMARK 465 HIS B 378
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 VAL A 24 CG1 CG2
REMARK 470 ASN A 114 CG OD1 ND2
REMARK 470 ARG A 194 CG CD NE CZ NH1 NH2
REMARK 470 VAL B 24 CG1 CG2
REMARK 470 LEU B 144 CG CD1 CD2
REMARK 470 ARG B 157 CG CD NE CZ NH1 NH2
REMARK 470 ASP B 159 CG OD1 OD2
REMARK 470 GLU B 335 CG CD OE1 OE2
REMARK 470 GLN B 369 CG CD OE1 NE2
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 OD1 ASN B 117 OG1 THR B 150 2.16
REMARK 500 O HOH B 522 O HOH B 614 2.18
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 ALA A 73 94.81 98.15
REMARK 500 SER A 145 119.35 -166.91
REMARK 500 SER A 145 116.36 -168.08
REMARK 500 ASP A 251 44.43 -91.37
REMARK 500 THR A 257 -162.79 -171.00
REMARK 500 ALA B 73 104.84 86.52
REMARK 500 ARG B 139 -173.05 -69.63
REMARK 500 ASP B 159 54.92 -95.01
REMARK 500 ASP B 247 0.24 -68.58
REMARK 500 ASP B 251 43.48 -89.39
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A 401 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 SER A 119 OG
REMARK 620 2 GLU A 252 OE2 88.1
REMARK 620 3 PRP A 402 O1A 96.7 174.4
REMARK 620 4 PRP A 402 O1B 90.1 85.5 97.2
REMARK 620 5 HOH A 505 O 165.8 84.9 89.8 101.7
REMARK 620 6 HOH A 533 O 75.1 79.5 98.9 159.1 91.5
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG B 401 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 SER B 119 OG
REMARK 620 2 GLU B 252 OE2 87.8
REMARK 620 3 PRP B 402 O2B 104.2 83.2
REMARK 620 4 PRP B 402 O1A 112.7 158.6 85.8
REMARK 620 5 PRP B 402 O1A 86.6 167.2 87.0 26.7
REMARK 620 6 PRP B 402 O2B 96.5 88.0 9.3 83.9 81.2
REMARK 620 7 HOH B 508 O 172.7 89.6 82.2 70.7 97.2 90.2
REMARK 620 8 HOH B 549 O 77.5 82.2 165.2 107.2 107.8 168.7 95.4
REMARK 620 N 1 2 3 4 5 6 7
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3QR9 RELATED DB: PDB
REMARK 900 3QR9 CONTAINS THE SAME PROTEIN WITH NO LIGANDS BOUND AND WAS USED
REMARK 900 IN MR FOR THIS STRUCTURE
REMARK 900 RELATED ID: 1ZVW RELATED DB: PDB
REMARK 900 1ZVW CONTAINS THE SAME PROTEIN CRYSTALLIZED IN DIFFERENT CONDITION
REMARK 900 AND WITH A DIFFERENT SPACE GROUP AND UNIT CELL, BUT WITH THE SAME
REMARK 900 LIGANDS
DBREF 5BYT A 2 370 UNP P9WFX5 TRPD_MYCTU 2 370
DBREF 5BYT B 2 370 UNP P9WFX5 TRPD_MYCTU 2 370
SEQADV 5BYT MET A 0 UNP P9WFX5 EXPRESSION TAG
SEQADV 5BYT VAL A 1 UNP P9WFX5 EXPRESSION TAG
SEQADV 5BYT LEU A 371 UNP P9WFX5 EXPRESSION TAG
SEQADV 5BYT GLU A 372 UNP P9WFX5 EXPRESSION TAG
SEQADV 5BYT HIS A 373 UNP P9WFX5 EXPRESSION TAG
SEQADV 5BYT HIS A 374 UNP P9WFX5 EXPRESSION TAG
SEQADV 5BYT HIS A 375 UNP P9WFX5 EXPRESSION TAG
SEQADV 5BYT HIS A 376 UNP P9WFX5 EXPRESSION TAG
SEQADV 5BYT HIS A 377 UNP P9WFX5 EXPRESSION TAG
SEQADV 5BYT HIS A 378 UNP P9WFX5 EXPRESSION TAG
SEQADV 5BYT MET B 0 UNP P9WFX5 EXPRESSION TAG
SEQADV 5BYT VAL B 1 UNP P9WFX5 EXPRESSION TAG
SEQADV 5BYT LEU B 371 UNP P9WFX5 EXPRESSION TAG
SEQADV 5BYT GLU B 372 UNP P9WFX5 EXPRESSION TAG
SEQADV 5BYT HIS B 373 UNP P9WFX5 EXPRESSION TAG
SEQADV 5BYT HIS B 374 UNP P9WFX5 EXPRESSION TAG
SEQADV 5BYT HIS B 375 UNP P9WFX5 EXPRESSION TAG
SEQADV 5BYT HIS B 376 UNP P9WFX5 EXPRESSION TAG
SEQADV 5BYT HIS B 377 UNP P9WFX5 EXPRESSION TAG
SEQADV 5BYT HIS B 378 UNP P9WFX5 EXPRESSION TAG
SEQRES 1 A 379 MET VAL ALA LEU SER ALA GLU GLY SER SER GLY GLY SER
SEQRES 2 A 379 ARG GLY GLY SER PRO LYS ALA GLU ALA ALA SER VAL PRO
SEQRES 3 A 379 SER TRP PRO GLN ILE LEU GLY ARG LEU THR ASP ASN ARG
SEQRES 4 A 379 ASP LEU ALA ARG GLY GLN ALA ALA TRP ALA MET ASP GLN
SEQRES 5 A 379 ILE MET THR GLY ASN ALA ARG PRO ALA GLN ILE ALA ALA
SEQRES 6 A 379 PHE ALA VAL ALA MET THR MET LYS ALA PRO THR ALA ASP
SEQRES 7 A 379 GLU VAL GLY GLU LEU ALA GLY VAL MET LEU SER HIS ALA
SEQRES 8 A 379 HIS PRO LEU PRO ALA ASP THR VAL PRO ASP ASP ALA VAL
SEQRES 9 A 379 ASP VAL VAL GLY THR GLY GLY ASP GLY VAL ASN THR VAL
SEQRES 10 A 379 ASN LEU SER THR MET ALA ALA ILE VAL VAL ALA ALA ALA
SEQRES 11 A 379 GLY VAL PRO VAL VAL LYS HIS GLY ASN ARG ALA ALA SER
SEQRES 12 A 379 SER LEU SER GLY GLY ALA ASP THR LEU GLU ALA LEU GLY
SEQRES 13 A 379 VAL ARG ILE ASP LEU GLY PRO ASP LEU VAL ALA ARG SER
SEQRES 14 A 379 LEU ALA GLU VAL GLY ILE GLY PHE CYS PHE ALA PRO ARG
SEQRES 15 A 379 PHE HIS PRO SER TYR ARG HIS ALA ALA ALA VAL ARG ARG
SEQRES 16 A 379 GLU ILE GLY VAL PRO THR VAL PHE ASN LEU LEU GLY PRO
SEQRES 17 A 379 LEU THR ASN PRO ALA ARG PRO ARG ALA GLY LEU ILE GLY
SEQRES 18 A 379 CYS ALA PHE ALA ASP LEU ALA GLU VAL MET ALA GLY VAL
SEQRES 19 A 379 PHE ALA ALA ARG ARG SER SER VAL LEU VAL VAL HIS GLY
SEQRES 20 A 379 ASP ASP GLY LEU ASP GLU LEU THR THR THR THR THR SER
SEQRES 21 A 379 THR ILE TRP ARG VAL ALA ALA GLY SER VAL ASP LYS LEU
SEQRES 22 A 379 THR PHE ASP PRO ALA GLY PHE GLY PHE ALA ARG ALA GLN
SEQRES 23 A 379 LEU ASP GLN LEU ALA GLY GLY ASP ALA GLN ALA ASN ALA
SEQRES 24 A 379 ALA ALA VAL ARG ALA VAL LEU GLY GLY ALA ARG GLY PRO
SEQRES 25 A 379 VAL ARG ASP ALA VAL VAL LEU ASN ALA ALA GLY ALA ILE
SEQRES 26 A 379 VAL ALA HIS ALA GLY LEU SER SER ARG ALA GLU TRP LEU
SEQRES 27 A 379 PRO ALA TRP GLU GLU GLY LEU ARG ARG ALA SER ALA ALA
SEQRES 28 A 379 ILE ASP THR GLY ALA ALA GLU GLN LEU LEU ALA ARG TRP
SEQRES 29 A 379 VAL ARG PHE GLY ARG GLN ILE LEU GLU HIS HIS HIS HIS
SEQRES 30 A 379 HIS HIS
SEQRES 1 B 379 MET VAL ALA LEU SER ALA GLU GLY SER SER GLY GLY SER
SEQRES 2 B 379 ARG GLY GLY SER PRO LYS ALA GLU ALA ALA SER VAL PRO
SEQRES 3 B 379 SER TRP PRO GLN ILE LEU GLY ARG LEU THR ASP ASN ARG
SEQRES 4 B 379 ASP LEU ALA ARG GLY GLN ALA ALA TRP ALA MET ASP GLN
SEQRES 5 B 379 ILE MET THR GLY ASN ALA ARG PRO ALA GLN ILE ALA ALA
SEQRES 6 B 379 PHE ALA VAL ALA MET THR MET LYS ALA PRO THR ALA ASP
SEQRES 7 B 379 GLU VAL GLY GLU LEU ALA GLY VAL MET LEU SER HIS ALA
SEQRES 8 B 379 HIS PRO LEU PRO ALA ASP THR VAL PRO ASP ASP ALA VAL
SEQRES 9 B 379 ASP VAL VAL GLY THR GLY GLY ASP GLY VAL ASN THR VAL
SEQRES 10 B 379 ASN LEU SER THR MET ALA ALA ILE VAL VAL ALA ALA ALA
SEQRES 11 B 379 GLY VAL PRO VAL VAL LYS HIS GLY ASN ARG ALA ALA SER
SEQRES 12 B 379 SER LEU SER GLY GLY ALA ASP THR LEU GLU ALA LEU GLY
SEQRES 13 B 379 VAL ARG ILE ASP LEU GLY PRO ASP LEU VAL ALA ARG SER
SEQRES 14 B 379 LEU ALA GLU VAL GLY ILE GLY PHE CYS PHE ALA PRO ARG
SEQRES 15 B 379 PHE HIS PRO SER TYR ARG HIS ALA ALA ALA VAL ARG ARG
SEQRES 16 B 379 GLU ILE GLY VAL PRO THR VAL PHE ASN LEU LEU GLY PRO
SEQRES 17 B 379 LEU THR ASN PRO ALA ARG PRO ARG ALA GLY LEU ILE GLY
SEQRES 18 B 379 CYS ALA PHE ALA ASP LEU ALA GLU VAL MET ALA GLY VAL
SEQRES 19 B 379 PHE ALA ALA ARG ARG SER SER VAL LEU VAL VAL HIS GLY
SEQRES 20 B 379 ASP ASP GLY LEU ASP GLU LEU THR THR THR THR THR SER
SEQRES 21 B 379 THR ILE TRP ARG VAL ALA ALA GLY SER VAL ASP LYS LEU
SEQRES 22 B 379 THR PHE ASP PRO ALA GLY PHE GLY PHE ALA ARG ALA GLN
SEQRES 23 B 379 LEU ASP GLN LEU ALA GLY GLY ASP ALA GLN ALA ASN ALA
SEQRES 24 B 379 ALA ALA VAL ARG ALA VAL LEU GLY GLY ALA ARG GLY PRO
SEQRES 25 B 379 VAL ARG ASP ALA VAL VAL LEU ASN ALA ALA GLY ALA ILE
SEQRES 26 B 379 VAL ALA HIS ALA GLY LEU SER SER ARG ALA GLU TRP LEU
SEQRES 27 B 379 PRO ALA TRP GLU GLU GLY LEU ARG ARG ALA SER ALA ALA
SEQRES 28 B 379 ILE ASP THR GLY ALA ALA GLU GLN LEU LEU ALA ARG TRP
SEQRES 29 B 379 VAL ARG PHE GLY ARG GLN ILE LEU GLU HIS HIS HIS HIS
SEQRES 30 B 379 HIS HIS
HET MG A 401 1
HET PRP A 402 22
HET MG B 401 1
HET PRP B 402 44
HETNAM MG MAGNESIUM ION
HETNAM PRP 1-O-PYROPHOSPHONO-5-O-PHOSPHONO-ALPHA-D-RIBOFURANOSE
HETSYN PRP ALPHA-PHOSPHORIBOSYLPYROPHOSPHORIC ACID; 1-O-
HETSYN 2 PRP PYROPHOSPHONO-5-O-PHOSPHONO-ALPHA-D-RIBOSE; 1-O-
HETSYN 3 PRP PYROPHOSPHONO-5-O-PHOSPHONO-D-RIBOSE; 1-O-
HETSYN 4 PRP PYROPHOSPHONO-5-O-PHOSPHONO-RIBOSE
FORMUL 3 MG 2(MG 2+)
FORMUL 4 PRP 2(C5 H13 O14 P3)
FORMUL 7 HOH *347(H2 O)
HELIX 1 AA1 SER A 26 ASP A 36 1 11
HELIX 2 AA2 GLY A 43 MET A 53 1 11
HELIX 3 AA3 ARG A 58 ALA A 73 1 16
HELIX 4 AA4 THR A 75 ALA A 90 1 16
HELIX 5 AA5 ASN A 117 ALA A 129 1 13
HELIX 6 AA6 GLY A 146 GLY A 155 1 10
HELIX 7 AA7 GLY A 161 GLY A 173 1 13
HELIX 8 AA8 ALA A 179 HIS A 183 1 5
HELIX 9 AA9 TYR A 186 GLY A 197 1 12
HELIX 10 AB1 THR A 200 ASN A 203 5 4
HELIX 11 AB2 LEU A 204 THR A 209 1 6
HELIX 12 AB3 PHE A 223 ARG A 237 1 15
HELIX 13 AB4 ASP A 275 GLY A 280 5 6
HELIX 14 AB5 GLN A 285 ALA A 290 5 6
HELIX 15 AB6 ASP A 293 GLY A 306 1 14
HELIX 16 AB7 GLY A 310 GLY A 329 1 20
HELIX 17 AB8 TRP A 336 THR A 353 1 18
HELIX 18 AB9 GLY A 354 GLN A 369 1 16
HELIX 19 AC1 SER B 26 ASP B 36 1 11
HELIX 20 AC2 GLY B 43 MET B 53 1 11
HELIX 21 AC3 ARG B 58 ALA B 73 1 16
HELIX 22 AC4 THR B 75 ALA B 90 1 16
HELIX 23 AC5 ASN B 117 ALA B 129 1 13
HELIX 24 AC6 GLY B 146 LEU B 154 1 9
HELIX 25 AC7 GLY B 161 VAL B 172 1 12
HELIX 26 AC8 ALA B 179 HIS B 183 1 5
HELIX 27 AC9 TYR B 186 GLY B 197 1 12
HELIX 28 AD1 THR B 200 ASN B 203 5 4
HELIX 29 AD2 LEU B 204 THR B 209 1 6
HELIX 30 AD3 LEU B 226 ARG B 237 1 12
HELIX 31 AD4 ASP B 275 GLY B 280 5 6
HELIX 32 AD5 ASP B 293 GLY B 306 1 14
HELIX 33 AD6 GLY B 310 GLY B 329 1 20
HELIX 34 AD7 TRP B 336 THR B 353 1 18
HELIX 35 AD8 GLY B 354 GLN B 369 1 16
SHEET 1 AA1 5 VAL A 103 GLY A 107 0
SHEET 2 AA1 5 ALA A 216 GLY A 220 1 O LEU A 218 N ASP A 104
SHEET 3 AA1 5 SER A 240 GLY A 246 1 O VAL A 244 N ILE A 219
SHEET 4 AA1 5 SER A 259 ALA A 265 -1 O VAL A 264 N VAL A 241
SHEET 5 AA1 5 SER A 268 PHE A 274 -1 O PHE A 274 N SER A 259
SHEET 1 AA2 2 VAL A 133 GLY A 137 0
SHEET 2 AA2 2 ILE A 174 PHE A 178 1 O CYS A 177 N LYS A 135
SHEET 1 AA3 5 VAL B 103 GLY B 107 0
SHEET 2 AA3 5 ALA B 216 GLY B 220 1 O LEU B 218 N ASP B 104
SHEET 3 AA3 5 SER B 240 GLY B 246 1 O VAL B 244 N ILE B 219
SHEET 4 AA3 5 SER B 259 ALA B 265 -1 O TRP B 262 N VAL B 243
SHEET 5 AA3 5 SER B 268 PHE B 274 -1 O PHE B 274 N SER B 259
SHEET 1 AA4 2 VAL B 133 GLY B 137 0
SHEET 2 AA4 2 ILE B 174 PHE B 178 1 O CYS B 177 N LYS B 135
LINK OG SER A 119 MG MG A 401 1555 1555 2.18
LINK OE2 GLU A 252 MG MG A 401 1555 1555 2.03
LINK MG MG A 401 O1A PRP A 402 1555 1555 2.03
LINK MG MG A 401 O1B PRP A 402 1555 1555 2.08
LINK MG MG A 401 O HOH A 505 1555 1555 2.25
LINK MG MG A 401 O HOH A 533 1555 1555 2.03
LINK OG SER B 119 MG MG B 401 1555 1555 2.08
LINK OE2 GLU B 252 MG MG B 401 1555 1555 2.03
LINK MG MG B 401 O2BAPRP B 402 1555 1555 2.23
LINK MG MG B 401 O1AAPRP B 402 1555 1555 1.99
LINK MG MG B 401 O1ABPRP B 402 1555 1555 2.31
LINK MG MG B 401 O2BBPRP B 402 1555 1555 2.27
LINK MG MG B 401 O HOH B 508 1555 1555 2.29
LINK MG MG B 401 O HOH B 549 1555 1555 2.17
CRYST1 112.011 81.192 78.578 90.00 90.00 90.00 P 21 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 0.008928 0.000000 0.000000 0.00000
SCALE2 0.000000 0.012316 0.000000 0.00000
SCALE3 0.000000 0.000000 0.012726 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
