HEADER HYDROLASE 08-SEP-17 6AYU
TITLE CRYSTAL STRUCTURE OF FRUCTOSE-1,6-BISPHOSPHATASE T84S FROM
TITLE 2 MYCOBACTERIUM TUBERCULOSIS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: FRUCTOSE-1,6-BISPHOSPHATASE CLASS 2;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: UNP RESIDUES 35-362;
COMPND 5 SYNONYM: FBPASE CLASS 2,D-FRUCTOSE-1,6-BISPHOSPHATE 1-
COMPND 6 PHOSPHOHYDROLASE CLASS 2;
COMPND 7 EC: 3.1.3.11;
COMPND 8 ENGINEERED: YES;
COMPND 9 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MYCOBACTERIUM TUBERCULOSIS;
SOURCE 3 ORGANISM_TAXID: 419947;
SOURCE 4 STRAIN: ATCC 25177 / H37RA;
SOURCE 5 ATCC: RV1099C;
SOURCE 6 GENE: GLPX, MRA_1110;
SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 9 EXPRESSION_SYSTEM_CELL: BL21 (DE3);
SOURCE 10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 11 EXPRESSION_SYSTEM_PLASMID: PET15B
KEYWDS FRUCTOSE-1, 6-BISPHOSPHATASE, GLUCONEOGENESIS, CLASS II PHOSPHATASE,
KEYWDS 2 MYCOBACTERIUM TUBERCULOSIS, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR C.ABAD-ZAPATERO,N.WOLF,H.J.GUTKA,F.MOVAHEDZADEH
REVDAT 4 04-OCT-23 6AYU 1 HETSYN
REVDAT 3 29-JUL-20 6AYU 1 COMPND REMARK HETNAM LINK
REVDAT 3 2 1 SITE
REVDAT 2 25-APR-18 6AYU 1 JRNL
REVDAT 1 14-MAR-18 6AYU 0
JRNL AUTH N.M.WOLF,H.J.GUTKA,F.MOVAHEDZADEH,C.ABAD-ZAPATERO
JRNL TITL STRUCTURES OF THE MYCOBACTERIUM TUBERCULOSIS GLPX PROTEIN
JRNL TITL 2 (CLASS II FRUCTOSE-1,6-BISPHOSPHATASE): IMPLICATIONS FOR THE
JRNL TITL 3 ACTIVE OLIGOMERIC STATE, CATALYTIC MECHANISM AND CITRATE
JRNL TITL 4 INHIBITION.
JRNL REF ACTA CRYSTALLOGR D STRUCT V. 74 321 2018
JRNL REF 2 BIOL
JRNL REFN ISSN 2059-7983
JRNL PMID 29652259
JRNL DOI 10.1107/S2059798318002838
REMARK 2
REMARK 2 RESOLUTION. 2.20 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (1.12_2829: ???)
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 : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.20
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 38.50
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 37420
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.206
REMARK 3 R VALUE (WORKING SET) : 0.204
REMARK 3 FREE R VALUE : 0.252
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.910
REMARK 3 FREE R VALUE TEST SET COUNT : 1839
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 38.5092 - 5.1566 1.00 2986 141 0.1923 0.2483
REMARK 3 2 5.1566 - 4.0945 1.00 2801 157 0.1701 0.1998
REMARK 3 3 4.0945 - 3.5773 1.00 2750 158 0.1811 0.2427
REMARK 3 4 3.5773 - 3.2504 1.00 2750 152 0.2110 0.2553
REMARK 3 5 3.2504 - 3.0176 1.00 2728 141 0.2226 0.2883
REMARK 3 6 3.0176 - 2.8397 1.00 2724 123 0.2274 0.2467
REMARK 3 7 2.8397 - 2.6975 1.00 2737 129 0.2354 0.2976
REMARK 3 8 2.6975 - 2.5801 1.00 2701 137 0.2323 0.2570
REMARK 3 9 2.5801 - 2.4808 1.00 2684 147 0.2484 0.2889
REMARK 3 10 2.4808 - 2.3952 1.00 2711 140 0.2487 0.3225
REMARK 3 11 2.3952 - 2.3203 1.00 2682 145 0.2525 0.3428
REMARK 3 12 2.3203 - 2.2540 1.00 2686 120 0.2556 0.3153
REMARK 3 13 2.2540 - 2.2000 0.99 2641 149 0.2531 0.2729
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
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) : 0.240
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 25.730
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 49.20
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 : 0.008 4767
REMARK 3 ANGLE : 1.020 6445
REMARK 3 CHIRALITY : 0.063 735
REMARK 3 PLANARITY : 0.005 847
REMARK 3 DIHEDRAL : 11.561 3371
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 6AYU COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 11-SEP-17.
REMARK 100 THE DEPOSITION ID IS D_1000229969.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 14-JUL-17
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 21-ID-G
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97872
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-3000
REMARK 200 DATA SCALING SOFTWARE : HKL-3000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 37421
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.200
REMARK 200 RESOLUTION RANGE LOW (A) : 40.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 10.80
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.08200
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 35.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.20
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.24
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 10.60
REMARK 200 R MERGE FOR SHELL (I) : 1.32600
REMARK 200 R SYM FOR SHELL (I) : 1.32600
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.100
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: 3D1R
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 48.96
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.41
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 2.4 M SODIUM MALONATE PH 6.0, VAPOR
REMARK 280 DIFFUSION, HANGING DROP, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 61 2 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+1/3
REMARK 290 3555 -X+Y,-X,Z+2/3
REMARK 290 4555 -X,-Y,Z+1/2
REMARK 290 5555 Y,-X+Y,Z+5/6
REMARK 290 6555 X-Y,X,Z+1/6
REMARK 290 7555 Y,X,-Z+1/3
REMARK 290 8555 X-Y,-Y,-Z
REMARK 290 9555 -X,-X+Y,-Z+2/3
REMARK 290 10555 -Y,-X,-Z+5/6
REMARK 290 11555 -X+Y,Y,-Z+1/2
REMARK 290 12555 X,X-Y,-Z+1/6
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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 47.61600
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 95.23200
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 71.42400
REMARK 290 SMTRY1 5 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 5 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 119.04000
REMARK 290 SMTRY1 6 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 23.80800
REMARK 290 SMTRY1 7 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 7 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 47.61600
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 9 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 9 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 9 0.000000 0.000000 -1.000000 95.23200
REMARK 290 SMTRY1 10 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 10 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 10 0.000000 0.000000 -1.000000 119.04000
REMARK 290 SMTRY1 11 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 11 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 11 0.000000 0.000000 -1.000000 71.42400
REMARK 290 SMTRY1 12 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 12 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 12 0.000000 0.000000 -1.000000 23.80800
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: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 16900 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 44020 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -48.0 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 350 BIOMT1 2 0.500000 -0.866025 0.000000 65.44500
REMARK 350 BIOMT2 2 -0.866025 -0.500000 0.000000 113.35407
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 -23.80800
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 GLY A -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 GLY A 319
REMARK 465 ASP A 320
REMARK 465 SER A 321
REMARK 465 SER A 322
REMARK 465 ALA A 323
REMARK 465 VAL A 324
REMARK 465 TYR A 325
REMARK 465 PRO A 326
REMARK 465 LEU A 327
REMARK 465 PRO A 328
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 SER B 307
REMARK 465 LYS B 308
REMARK 465 LEU B 309
REMARK 465 ASN B 310
REMARK 465 GLU B 311
REMARK 465 TYR B 312
REMARK 465 SER B 313
REMARK 465 ALA B 314
REMARK 465 ILE B 315
REMARK 465 ASP B 316
REMARK 465 PHE B 317
REMARK 465 THR B 318
REMARK 465 GLY B 319
REMARK 465 ASP B 320
REMARK 465 SER B 321
REMARK 465 SER B 322
REMARK 465 ALA B 323
REMARK 465 VAL B 324
REMARK 465 TYR B 325
REMARK 465 PRO B 326
REMARK 465 LEU B 327
REMARK 465 PRO B 328
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 507 O HOH A 545 1.96
REMARK 500 NH2 ARG A 170 O HOH A 501 1.98
REMARK 500 O GLY B 19 O HOH A 501 2.03
REMARK 500 O HOH A 522 O HOH A 536 2.06
REMARK 500 NH2 ARG A 217 O GLY A 257 2.10
REMARK 500 O HOH A 522 O HOH A 539 2.11
REMARK 500 NZ LYS B 293 O HOH B 501 2.13
REMARK 500 O HOH B 509 O HOH B 511 2.16
REMARK 500 O HOH A 501 O HOH B 535 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 LYS A 54 -10.93 -34.66
REMARK 500 HIS A 56 -6.10 -58.85
REMARK 500 SER A 307 -101.54 -179.01
REMARK 500 ASN A 310 -9.96 71.51
REMARK 500 ALA B 57 96.69 -161.25
REMARK 500 ASP B 70 -168.53 -78.49
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 LEU A 306 SER A 307 131.31
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 402 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 79 OD2
REMARK 620 2 ASP A 82 OD1 90.4
REMARK 620 3 GLU A 208 OE2 106.2 113.0
REMARK 620 4 GOL A 407 O2 95.2 145.3 98.3
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A 406 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 SER A 189 O
REMARK 620 2 ALA A 190 O 71.6
REMARK 620 3 ARG A 192 O 87.3 93.0
REMARK 620 4 SER A 195 OG 51.5 123.1 87.8
REMARK 620 5 THR A 197 O 81.6 86.5 168.5 82.9
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG B 403 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 79 OD2
REMARK 620 2 ASP B 82 OD1 101.8
REMARK 620 3 GLU B 208 OE2 102.3 120.6
REMARK 620 N 1 2
DBREF 6AYU A 1 328 UNP A5U1E6 GLPX_MYCTA 35 362
DBREF 6AYU B 1 328 UNP A5U1E6 GLPX_MYCTA 35 362
SEQADV 6AYU GLY A -18 UNP A5U1E6 EXPRESSION TAG
SEQADV 6AYU SER A -17 UNP A5U1E6 EXPRESSION TAG
SEQADV 6AYU SER A -16 UNP A5U1E6 EXPRESSION TAG
SEQADV 6AYU HIS A -15 UNP A5U1E6 EXPRESSION TAG
SEQADV 6AYU HIS A -14 UNP A5U1E6 EXPRESSION TAG
SEQADV 6AYU HIS A -13 UNP A5U1E6 EXPRESSION TAG
SEQADV 6AYU HIS A -12 UNP A5U1E6 EXPRESSION TAG
SEQADV 6AYU HIS A -11 UNP A5U1E6 EXPRESSION TAG
SEQADV 6AYU HIS A -10 UNP A5U1E6 EXPRESSION TAG
SEQADV 6AYU SER A -9 UNP A5U1E6 EXPRESSION TAG
SEQADV 6AYU SER A -8 UNP A5U1E6 EXPRESSION TAG
SEQADV 6AYU GLY A -7 UNP A5U1E6 EXPRESSION TAG
SEQADV 6AYU LEU A -6 UNP A5U1E6 EXPRESSION TAG
SEQADV 6AYU VAL A -5 UNP A5U1E6 EXPRESSION TAG
SEQADV 6AYU PRO A -4 UNP A5U1E6 EXPRESSION TAG
SEQADV 6AYU ARG A -3 UNP A5U1E6 EXPRESSION TAG
SEQADV 6AYU GLY A -2 UNP A5U1E6 EXPRESSION TAG
SEQADV 6AYU SER A -1 UNP A5U1E6 EXPRESSION TAG
SEQADV 6AYU HIS A 0 UNP A5U1E6 EXPRESSION TAG
SEQADV 6AYU SER A 84 UNP A5U1E6 THR 118 ENGINEERED MUTATION
SEQADV 6AYU GLY B -18 UNP A5U1E6 EXPRESSION TAG
SEQADV 6AYU SER B -17 UNP A5U1E6 EXPRESSION TAG
SEQADV 6AYU SER B -16 UNP A5U1E6 EXPRESSION TAG
SEQADV 6AYU HIS B -15 UNP A5U1E6 EXPRESSION TAG
SEQADV 6AYU HIS B -14 UNP A5U1E6 EXPRESSION TAG
SEQADV 6AYU HIS B -13 UNP A5U1E6 EXPRESSION TAG
SEQADV 6AYU HIS B -12 UNP A5U1E6 EXPRESSION TAG
SEQADV 6AYU HIS B -11 UNP A5U1E6 EXPRESSION TAG
SEQADV 6AYU HIS B -10 UNP A5U1E6 EXPRESSION TAG
SEQADV 6AYU SER B -9 UNP A5U1E6 EXPRESSION TAG
SEQADV 6AYU SER B -8 UNP A5U1E6 EXPRESSION TAG
SEQADV 6AYU GLY B -7 UNP A5U1E6 EXPRESSION TAG
SEQADV 6AYU LEU B -6 UNP A5U1E6 EXPRESSION TAG
SEQADV 6AYU VAL B -5 UNP A5U1E6 EXPRESSION TAG
SEQADV 6AYU PRO B -4 UNP A5U1E6 EXPRESSION TAG
SEQADV 6AYU ARG B -3 UNP A5U1E6 EXPRESSION TAG
SEQADV 6AYU GLY B -2 UNP A5U1E6 EXPRESSION TAG
SEQADV 6AYU SER B -1 UNP A5U1E6 EXPRESSION TAG
SEQADV 6AYU HIS B 0 UNP A5U1E6 EXPRESSION TAG
SEQADV 6AYU SER B 84 UNP A5U1E6 THR 118 ENGINEERED MUTATION
SEQRES 1 A 347 GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY LEU
SEQRES 2 A 347 VAL PRO ARG GLY SER HIS MET GLU LEU VAL ARG VAL THR
SEQRES 3 A 347 GLU ALA GLY ALA MET ALA ALA GLY ARG TRP VAL GLY ARG
SEQRES 4 A 347 GLY ASP LYS GLU GLY GLY ASP GLY ALA ALA VAL ASP ALA
SEQRES 5 A 347 MET ARG GLU LEU VAL ASN SER VAL SER MET ARG GLY VAL
SEQRES 6 A 347 VAL VAL ILE GLY GLU GLY GLU LYS ASP HIS ALA PRO MET
SEQRES 7 A 347 LEU TYR ASN GLY GLU GLU VAL GLY ASN GLY ASP GLY PRO
SEQRES 8 A 347 GLU CYS ASP PHE ALA VAL ASP PRO ILE ASP GLY SER THR
SEQRES 9 A 347 LEU MET SER LYS GLY MET THR ASN ALA ILE SER VAL LEU
SEQRES 10 A 347 ALA VAL ALA ASP ARG GLY THR MET PHE ASP PRO SER ALA
SEQRES 11 A 347 VAL PHE TYR MET ASN LYS ILE ALA VAL GLY PRO ASP ALA
SEQRES 12 A 347 ALA HIS VAL LEU ASP ILE THR ALA PRO ILE SER GLU ASN
SEQRES 13 A 347 ILE ARG ALA VAL ALA LYS VAL LYS ASP LEU SER VAL ARG
SEQRES 14 A 347 ASP MET THR VAL CYS ILE LEU ASP ARG PRO ARG HIS ALA
SEQRES 15 A 347 GLN LEU ILE HIS ASP VAL ARG ALA THR GLY ALA ARG ILE
SEQRES 16 A 347 ARG LEU ILE THR ASP GLY ASP VAL ALA GLY ALA ILE SER
SEQRES 17 A 347 ALA CYS ARG PRO HIS SER GLY THR ASP LEU LEU ALA GLY
SEQRES 18 A 347 ILE GLY GLY THR PRO GLU GLY ILE ILE ALA ALA ALA ALA
SEQRES 19 A 347 ILE ARG CYS MET GLY GLY ALA ILE GLN ALA GLN LEU ALA
SEQRES 20 A 347 PRO ARG ASP ASP ALA GLU ARG ARG LYS ALA LEU GLU ALA
SEQRES 21 A 347 GLY TYR ASP LEU ASN GLN VAL LEU THR THR GLU ASP LEU
SEQRES 22 A 347 VAL SER GLY GLU ASN VAL PHE PHE CYS ALA THR GLY VAL
SEQRES 23 A 347 THR ASP GLY ASP LEU LEU LYS GLY VAL ARG TYR TYR PRO
SEQRES 24 A 347 GLY GLY CYS THR THR HIS SER ILE VAL MET ARG SER LYS
SEQRES 25 A 347 SER GLY THR VAL ARG MET ILE GLU ALA TYR HIS ARG LEU
SEQRES 26 A 347 SER LYS LEU ASN GLU TYR SER ALA ILE ASP PHE THR GLY
SEQRES 27 A 347 ASP SER SER ALA VAL TYR PRO LEU PRO
SEQRES 1 B 347 GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY LEU
SEQRES 2 B 347 VAL PRO ARG GLY SER HIS MET GLU LEU VAL ARG VAL THR
SEQRES 3 B 347 GLU ALA GLY ALA MET ALA ALA GLY ARG TRP VAL GLY ARG
SEQRES 4 B 347 GLY ASP LYS GLU GLY GLY ASP GLY ALA ALA VAL ASP ALA
SEQRES 5 B 347 MET ARG GLU LEU VAL ASN SER VAL SER MET ARG GLY VAL
SEQRES 6 B 347 VAL VAL ILE GLY GLU GLY GLU LYS ASP HIS ALA PRO MET
SEQRES 7 B 347 LEU TYR ASN GLY GLU GLU VAL GLY ASN GLY ASP GLY PRO
SEQRES 8 B 347 GLU CYS ASP PHE ALA VAL ASP PRO ILE ASP GLY SER THR
SEQRES 9 B 347 LEU MET SER LYS GLY MET THR ASN ALA ILE SER VAL LEU
SEQRES 10 B 347 ALA VAL ALA ASP ARG GLY THR MET PHE ASP PRO SER ALA
SEQRES 11 B 347 VAL PHE TYR MET ASN LYS ILE ALA VAL GLY PRO ASP ALA
SEQRES 12 B 347 ALA HIS VAL LEU ASP ILE THR ALA PRO ILE SER GLU ASN
SEQRES 13 B 347 ILE ARG ALA VAL ALA LYS VAL LYS ASP LEU SER VAL ARG
SEQRES 14 B 347 ASP MET THR VAL CYS ILE LEU ASP ARG PRO ARG HIS ALA
SEQRES 15 B 347 GLN LEU ILE HIS ASP VAL ARG ALA THR GLY ALA ARG ILE
SEQRES 16 B 347 ARG LEU ILE THR ASP GLY ASP VAL ALA GLY ALA ILE SER
SEQRES 17 B 347 ALA CYS ARG PRO HIS SER GLY THR ASP LEU LEU ALA GLY
SEQRES 18 B 347 ILE GLY GLY THR PRO GLU GLY ILE ILE ALA ALA ALA ALA
SEQRES 19 B 347 ILE ARG CYS MET GLY GLY ALA ILE GLN ALA GLN LEU ALA
SEQRES 20 B 347 PRO ARG ASP ASP ALA GLU ARG ARG LYS ALA LEU GLU ALA
SEQRES 21 B 347 GLY TYR ASP LEU ASN GLN VAL LEU THR THR GLU ASP LEU
SEQRES 22 B 347 VAL SER GLY GLU ASN VAL PHE PHE CYS ALA THR GLY VAL
SEQRES 23 B 347 THR ASP GLY ASP LEU LEU LYS GLY VAL ARG TYR TYR PRO
SEQRES 24 B 347 GLY GLY CYS THR THR HIS SER ILE VAL MET ARG SER LYS
SEQRES 25 B 347 SER GLY THR VAL ARG MET ILE GLU ALA TYR HIS ARG LEU
SEQRES 26 B 347 SER LYS LEU ASN GLU TYR SER ALA ILE ASP PHE THR GLY
SEQRES 27 B 347 ASP SER SER ALA VAL TYR PRO LEU PRO
HET F6P A 401 16
HET MG A 402 1
HET MLI A 403 7
HET GOL A 404 6
HET GOL A 405 6
HET MG A 406 1
HET GOL A 407 6
HET F6P B 401 16
HET GOL B 402 6
HET MG B 403 1
HET GOL B 404 6
HET GOL B 405 6
HET GOL B 406 6
HETNAM F6P 6-O-PHOSPHONO-BETA-D-FRUCTOFURANOSE
HETNAM MG MAGNESIUM ION
HETNAM MLI MALONATE ION
HETNAM GOL GLYCEROL
HETSYN F6P FRUCTOSE-6-PHOSPHATE; 6-O-PHOSPHONO-BETA-D-FRUCTOSE; 6-
HETSYN 2 F6P O-PHOSPHONO-D-FRUCTOSE; 6-O-PHOSPHONO-FRUCTOSE
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 3 F6P 2(C6 H13 O9 P)
FORMUL 4 MG 3(MG 2+)
FORMUL 5 MLI C3 H2 O4 2-
FORMUL 6 GOL 7(C3 H8 O3)
FORMUL 16 HOH *164(H2 O)
HELIX 1 AA1 HIS A 0 GLU A 2 5 3
HELIX 2 AA2 LEU A 3 ARG A 16 1 14
HELIX 3 AA3 ASP A 22 SER A 40 1 19
HELIX 4 AA4 GLY A 83 GLY A 90 1 8
HELIX 5 AA5 GLY A 121 ALA A 125 5 5
HELIX 6 AA6 PRO A 133 LYS A 145 1 13
HELIX 7 AA7 SER A 148 ASP A 151 5 4
HELIX 8 AA8 ARG A 159 ARG A 161 5 3
HELIX 9 AA9 HIS A 162 GLY A 173 1 12
HELIX 10 AB1 GLY A 182 ARG A 192 1 11
HELIX 11 AB2 THR A 206 GLY A 220 1 15
HELIX 12 AB3 ASP A 231 ALA A 241 1 11
HELIX 13 AB4 THR A 251 VAL A 255 1 5
HELIX 14 AB5 HIS B 0 GLU B 2 5 3
HELIX 15 AB6 LEU B 3 ARG B 16 1 14
HELIX 16 AB7 ASP B 22 ASN B 39 1 18
HELIX 17 AB8 GLY B 83 LYS B 89 1 7
HELIX 18 AB9 ALA B 124 LEU B 128 5 5
HELIX 19 AC1 PRO B 133 ASP B 146 1 14
HELIX 20 AC2 SER B 148 ASP B 151 5 4
HELIX 21 AC3 ARG B 159 ARG B 161 5 3
HELIX 22 AC4 HIS B 162 GLY B 173 1 12
HELIX 23 AC5 GLY B 182 ARG B 192 1 11
HELIX 24 AC6 THR B 206 GLY B 220 1 15
HELIX 25 AC7 ASP B 231 GLU B 240 1 10
HELIX 26 AC8 THR B 250 VAL B 255 1 6
SHEET 1 AA1 7 GLU A 65 VAL A 66 0
SHEET 2 AA1 7 ARG A 44 ILE A 49 -1 N GLY A 45 O VAL A 66
SHEET 3 AA1 7 GLU A 73 ASP A 79 1 O PHE A 76 N VAL A 48
SHEET 4 AA1 7 ILE A 95 ASP A 102 -1 O ALA A 99 N ALA A 77
SHEET 5 AA1 7 PHE A 261 GLY A 266 -1 O PHE A 261 N VAL A 100
SHEET 6 AA1 7 GLY A 282 ARG A 291 -1 O HIS A 286 N GLY A 266
SHEET 7 AA1 7 ARG A 277 TYR A 278 -1 N ARG A 277 O THR A 284
SHEET 1 AA2 7 GLU A 65 VAL A 66 0
SHEET 2 AA2 7 ARG A 44 ILE A 49 -1 N GLY A 45 O VAL A 66
SHEET 3 AA2 7 GLU A 73 ASP A 79 1 O PHE A 76 N VAL A 48
SHEET 4 AA2 7 ILE A 95 ASP A 102 -1 O ALA A 99 N ALA A 77
SHEET 5 AA2 7 PHE A 261 GLY A 266 -1 O PHE A 261 N VAL A 100
SHEET 6 AA2 7 GLY A 282 ARG A 291 -1 O HIS A 286 N GLY A 266
SHEET 7 AA2 7 VAL A 297 ARG A 305 -1 O ARG A 298 N VAL A 289
SHEET 1 AA3 6 ARG A 175 ILE A 179 0
SHEET 2 AA3 6 THR A 153 LEU A 157 1 N VAL A 154 O ARG A 175
SHEET 3 AA3 6 LEU A 199 GLY A 205 1 O LEU A 199 N CYS A 155
SHEET 4 AA3 6 TYR A 114 VAL A 120 -1 N MET A 115 O GLY A 204
SHEET 5 AA3 6 ALA A 222 LEU A 227 -1 O GLN A 226 N ASN A 116
SHEET 6 AA3 6 LEU A 249 THR A 250 -1 O LEU A 249 N ALA A 225
SHEET 1 AA4 7 GLU B 65 VAL B 66 0
SHEET 2 AA4 7 ARG B 44 ILE B 49 -1 N GLY B 45 O VAL B 66
SHEET 3 AA4 7 GLU B 73 ASP B 79 1 O VAL B 78 N ILE B 49
SHEET 4 AA4 7 ILE B 95 ASP B 102 -1 O ALA B 99 N ALA B 77
SHEET 5 AA4 7 PHE B 261 GLY B 266 -1 O PHE B 261 N VAL B 100
SHEET 6 AA4 7 GLY B 282 ARG B 291 -1 O HIS B 286 N GLY B 266
SHEET 7 AA4 7 ARG B 277 TYR B 278 -1 N ARG B 277 O THR B 284
SHEET 1 AA5 7 GLU B 65 VAL B 66 0
SHEET 2 AA5 7 ARG B 44 ILE B 49 -1 N GLY B 45 O VAL B 66
SHEET 3 AA5 7 GLU B 73 ASP B 79 1 O VAL B 78 N ILE B 49
SHEET 4 AA5 7 ILE B 95 ASP B 102 -1 O ALA B 99 N ALA B 77
SHEET 5 AA5 7 PHE B 261 GLY B 266 -1 O PHE B 261 N VAL B 100
SHEET 6 AA5 7 GLY B 282 ARG B 291 -1 O HIS B 286 N GLY B 266
SHEET 7 AA5 7 VAL B 297 ARG B 305 -1 O ARG B 298 N VAL B 289
SHEET 1 AA6 5 ARG B 175 ILE B 179 0
SHEET 2 AA6 5 THR B 153 LEU B 157 1 N VAL B 154 O ARG B 177
SHEET 3 AA6 5 LEU B 199 GLY B 205 1 O LEU B 199 N CYS B 155
SHEET 4 AA6 5 TYR B 114 VAL B 120 -1 N MET B 115 O GLY B 204
SHEET 5 AA6 5 ALA B 222 LEU B 227 -1 O GLN B 224 N ILE B 118
LINK OD2 ASP A 79 MG MG A 402 1555 1555 2.38
LINK OD1 ASP A 82 MG MG A 402 1555 1555 2.78
LINK O SER A 189 MG MG A 406 1555 1555 2.85
LINK O ALA A 190 MG MG A 406 1555 1555 2.83
LINK O ARG A 192 MG MG A 406 1555 1555 2.30
LINK OG SER A 195 MG MG A 406 1555 1555 2.76
LINK O THR A 197 MG MG A 406 1555 1555 2.35
LINK OE2 GLU A 208 MG MG A 402 1555 1555 2.74
LINK MG MG A 402 O2 GOL A 407 1555 1555 2.98
LINK OD2 ASP B 79 MG MG B 403 1555 1555 2.26
LINK OD1 ASP B 82 MG MG B 403 1555 1555 2.37
LINK OE2 GLU B 208 MG MG B 403 1555 1555 2.80
CISPEP 1 ASN B 68 GLY B 69 0 4.72
CRYST1 130.890 130.890 142.848 90.00 90.00 120.00 P 61 2 2 24
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 0.007640 0.004411 0.000000 0.00000
SCALE2 0.000000 0.008822 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007000 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
