HEADER TRANSFERASE 12-MAR-13 4BES
TITLE CRYSTAL STRUCTURE OF THE LEGIONELLA PNEUMOPHILA FIC DOMAIN-CONTAINING
TITLE 2 EFFECTOR ANKX PROTEIN IN COMPLEX WITH CYTIDINE MONOPHOSPHATE AND
TITLE 3 PHOSPHOCHOLINE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PHOSPHOCHOLINE TRANSFERASE ANKX;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: FIC AND ANKYRIN REPEATS DOMAINS, RESIDUES 2-484;
COMPND 5 SYNONYM: PC TRANSFERASE, ANKYRIN REPEAT-CONTAINING PROTEIN X;
COMPND 6 EC: 2.7.1.-;
COMPND 7 ENGINEERED: YES;
COMPND 8 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: LEGIONELLA PNEUMOPHILA SUBSP. PNEUMOPHILA STR.
SOURCE 3 PHILADELPHIA 1;
SOURCE 4 ORGANISM_TAXID: 272624;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_VARIANT: ROSETTA PLYSS;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_VECTOR: PDEST17
KEYWDS TRANSFERASE, PHOSPHOCHOLINATION, TYPE IV SECRETION SYSTEM EFFECTOR
EXPDTA X-RAY DIFFRACTION
AUTHOR V.CAMPANACCI,S.MUKHERJEE,C.R.ROY,J.CHERFILS
REVDAT 3 20-DEC-23 4BES 1 REMARK
REVDAT 2 29-MAY-13 4BES 1 JRNL
REVDAT 1 24-APR-13 4BES 0
JRNL AUTH V.CAMPANACCI,S.MUKHERJEE,C.R.ROY,J.CHERFILS
JRNL TITL STRUCTURE OF THE LEGIONELLA EFFECTOR ANKX REVEALS THE
JRNL TITL 2 MECHANISM OF PHOSPHOCHOLINE TRANSFER BY THE FIC DOMAIN.
JRNL REF EMBO J. V. 32 1469 2013
JRNL REFN ISSN 0261-4189
JRNL PMID 23572077
JRNL DOI 10.1038/EMBOJ.2013.82
REMARK 2
REMARK 2 RESOLUTION. 2.54 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : BUSTER 2.10.0
REMARK 3 AUTHORS : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER,
REMARK 3 : PACIOREK,ROVERSI,SHARFF,SMART,VONRHEIN,
REMARK 3 : WOMACK,MATTHEWS,TEN EYCK,TRONRUD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.54
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 43.10
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 3 NUMBER OF REFLECTIONS : 19367
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING + TEST SET) : 0.204
REMARK 3 R VALUE (WORKING SET) : 0.201
REMARK 3 FREE R VALUE : 0.259
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.380
REMARK 3 FREE R VALUE TEST SET COUNT : 1041
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 10
REMARK 3 BIN RESOLUTION RANGE HIGH (ANGSTROMS) : 2.54
REMARK 3 BIN RESOLUTION RANGE LOW (ANGSTROMS) : 2.68
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.71
REMARK 3 REFLECTIONS IN BIN (WORKING + TEST SET) : 2761
REMARK 3 BIN R VALUE (WORKING + TEST SET) : 0.2231
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 2606
REMARK 3 BIN R VALUE (WORKING SET) : 0.2198
REMARK 3 BIN FREE R VALUE : 0.2786
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5.61
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 155
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3736
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 47
REMARK 3 SOLVENT ATOMS : 54
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 55.92
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 55.86
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.08110
REMARK 3 B22 (A**2) : 10.59720
REMARK 3 B33 (A**2) : -10.51610
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.328
REMARK 3 DPI (BLOW EQ-10) BASED ON R VALUE (A) : 0.511
REMARK 3 DPI (BLOW EQ-9) BASED ON FREE R VALUE (A) : 0.289
REMARK 3 DPI (CRUICKSHANK) BASED ON R VALUE (A) : 0.504
REMARK 3 DPI (CRUICKSHANK) BASED ON FREE R VALUE (A) : 0.292
REMARK 3
REMARK 3 REFERENCES: BLOW, D. (2002) ACTA CRYST D58, 792-797
REMARK 3 CRUICKSHANK, D.W.J. (1999) ACTA CRYST D55, 583-601
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.924
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.889
REMARK 3
REMARK 3 NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15
REMARK 3 TERM COUNT WEIGHT FUNCTION.
REMARK 3 BOND LENGTHS : 3895 ; 2.000 ; HARMONIC
REMARK 3 BOND ANGLES : 5289 ; 2.000 ; HARMONIC
REMARK 3 TORSION ANGLES : 1365 ; 2.000 ; SINUSOIDAL
REMARK 3 TRIGONAL CARBON PLANES : 105 ; 2.000 ; HARMONIC
REMARK 3 GENERAL PLANES : 554 ; 5.000 ; HARMONIC
REMARK 3 ISOTROPIC THERMAL FACTORS : 3895 ; 20.000 ; HARMONIC
REMARK 3 BAD NON-BONDED CONTACTS : NULL ; NULL ; NULL
REMARK 3 IMPROPER TORSIONS : NULL ; NULL ; NULL
REMARK 3 PSEUDOROTATION ANGLES : NULL ; NULL ; NULL
REMARK 3 CHIRAL IMPROPER TORSION : 491 ; 5.000 ; SEMIHARMONIC
REMARK 3 SUM OF OCCUPANCIES : NULL ; NULL ; NULL
REMARK 3 UTILITY DISTANCES : NULL ; NULL ; NULL
REMARK 3 UTILITY ANGLES : NULL ; NULL ; NULL
REMARK 3 UTILITY TORSION : NULL ; NULL ; NULL
REMARK 3 IDEAL-DIST CONTACT TERM : 4532 ; 4.000 ; SEMIHARMONIC
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.010
REMARK 3 BOND ANGLES (DEGREES) : 1.21
REMARK 3 PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 2.78
REMARK 3 OTHER TORSION ANGLES (DEGREES) : 22.74
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 3
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN A AND RESSEQ 6-220
REMARK 3 ORIGIN FOR THE GROUP (A): -17.1342 30.9185 1.5129
REMARK 3 T TENSOR
REMARK 3 T11: -0.2865 T22: -0.3444
REMARK 3 T33: -0.1544 T12: 0.0349
REMARK 3 T13: -0.0717 T23: -0.0193
REMARK 3 L TENSOR
REMARK 3 L11: 1.5964 L22: 1.8322
REMARK 3 L33: 1.2061 L12: 0.2032
REMARK 3 L13: -0.0896 L23: -0.0147
REMARK 3 S TENSOR
REMARK 3 S11: -0.0070 S12: -0.1168 S13: 0.2343
REMARK 3 S21: 0.2041 S22: 0.0590 S23: -0.0226
REMARK 3 S31: -0.1808 S32: 0.0652 S33: -0.0520
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN A AND RESSEQ 221-351
REMARK 3 ORIGIN FOR THE GROUP (A): -19.7827 17.1397 7.3827
REMARK 3 T TENSOR
REMARK 3 T11: -0.1897 T22: -0.2772
REMARK 3 T33: -0.1197 T12: 0.0507
REMARK 3 T13: -0.0423 T23: 0.0173
REMARK 3 L TENSOR
REMARK 3 L11: 1.4185 L22: 1.6497
REMARK 3 L33: 1.4427 L12: -0.7728
REMARK 3 L13: -0.0226 L23: 0.2378
REMARK 3 S TENSOR
REMARK 3 S11: -0.1372 S12: -0.1507 S13: -0.2017
REMARK 3 S21: 0.3904 S22: 0.1151 S23: -0.0532
REMARK 3 S31: 0.1381 S32: 0.0575 S33: 0.0221
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN A AND RESSEQ 352-484
REMARK 3 ORIGIN FOR THE GROUP (A): -12.1856 6.2205 -15.2052
REMARK 3 T TENSOR
REMARK 3 T11: -0.2620 T22: -0.3374
REMARK 3 T33: -0.1861 T12: -0.0005
REMARK 3 T13: 0.0007 T23: -0.0302
REMARK 3 L TENSOR
REMARK 3 L11: 1.8033 L22: 1.7025
REMARK 3 L33: 0.6349 L12: -0.6046
REMARK 3 L13: -0.4319 L23: -0.2950
REMARK 3 S TENSOR
REMARK 3 S11: 0.0148 S12: 0.1674 S13: -0.0845
REMARK 3 S21: -0.2909 S22: 0.0183 S23: 0.0039
REMARK 3 S31: 0.0038 S32: 0.0622 S33: -0.0331
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: IDEAL-DIST CONTACT TERM CONTACT SETUP.
REMARK 3 ALL ATOMS HAVE CCP4 ATOM TYPE FROM LIBRARY
REMARK 4
REMARK 4 4BES COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 12-MAR-13.
REMARK 100 THE DEPOSITION ID IS D_1290056081.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 22-MAR-12
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SOLEIL
REMARK 200 BEAMLINE : PROXIMA 1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9801
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XDS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 19367
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.540
REMARK 200 RESOLUTION RANGE LOW (A) : 43.100
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 200 DATA REDUNDANCY : 5.800
REMARK 200 R MERGE (I) : 0.10000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 13.4200
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.54
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.68
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.8
REMARK 200 DATA REDUNDANCY IN SHELL : 5.70
REMARK 200 R MERGE FOR SHELL (I) : 0.75000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.500
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 4BEP
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 49.45
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.43
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M AMMONIUM SULFATE, 30% PEG 5000
REMARK 280 MME, 0.1 M MES PH 6.5
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 42.13750
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 61.15200
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 42.13750
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 61.15200
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: 5540 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 39460 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -111.1 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 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 GLY A 1
REMARK 465 VAL A 2
REMARK 465 LYS A 3
REMARK 465 ILE A 4
REMARK 465 MET A 5
REMARK 465 LYS A 86
REMARK 465 LYS A 87
REMARK 465 VAL A 88
REMARK 465 GLU A 89
REMARK 465 GLU A 90
REMARK 465 LEU A 91
REMARK 465 GLN A 92
REMARK 465 GLU A 93
REMARK 465 LYS A 94
REMARK 465 ASN A 95
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 LYS A 324 CG CD CE NZ
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 SER A 66 121.87 -171.23
REMARK 500 THR A 101 -71.75 -114.02
REMARK 500 ASN A 242 -82.34 -118.58
REMARK 500 PHE A 264 30.37 -83.86
REMARK 500 PHE A 328 42.70 -105.88
REMARK 500 ASP A 330 30.59 -86.33
REMARK 500 GLU A 349 52.00 -101.33
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 A2054 DISTANCE = 5.84 ANGSTROMS
REMARK 600
REMARK 600 HETEROGEN
REMARK 600
REMARK 600 PHOSPHOCHOLINE (PC): PRODUCED AFTER ADDITION OF CDP-CHOLINE
REMARK 600 CYTIDINE-5'-MONOPHOSPHATE (C5P): PRODUCED AFTER ADDITION OF
REMARK 600 CDP-CHOLINE
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE C5P A 1000
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PC A 2000
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 3000
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 3001
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 3002
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4BEP RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE LEGIONELLA PNEUMOPHILA FIC DOMAIN-
REMARK 900 CONTAINING EFFECTOR ANKX PROTEIN (APO-FORM)
REMARK 900 RELATED ID: 4BER RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE LEGIONELLA PNEUMOPHILA FIC DOMAIN-
REMARK 900 CONTAINING EFFECTOR ANKX PROTEIN IN COMPLEX WITH CYTIDINE
REMARK 900 MONOPHOSPHATE
REMARK 900 RELATED ID: 4BET RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE LEGIONELLA PNEUMOPHILA FIC DOMAIN-
REMARK 900 CONTAINING EFFECTOR ANKX PROTEIN (INACTIVE H229A MUTANT) IN COMPLEX
REMARK 900 WITH CYTIDINE-DIPHOSPHATE-CHOLINE
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 L247P (CLONING ARTEFACT)
DBREF 4BES A 2 484 UNP Q5ZXN6 ANKX_LEGPH 2 484
SEQADV 4BES GLY A 1 UNP Q5ZXN6 EXPRESSION TAG
SEQADV 4BES PRO A 247 UNP Q5ZXN6 LEU 247 ENGINEERED MUTATION
SEQRES 1 A 484 GLY VAL LYS ILE MET PRO ASN LEU PRO GLY LEU TYR PHE
SEQRES 2 A 484 LEU GLN ALA TYR PRO SER GLU GLU ILE TRP ARG LEU PHE
SEQRES 3 A 484 VAL ASP GLY ARG PHE TRP SER LYS GLU ASN GLY TRP ARG
SEQRES 4 A 484 GLY TYR GLU SER ARG GLU PRO GLY CYS LEU ASN ALA ALA
SEQRES 5 A 484 LEU GLU SER LEU CYS SER ILE ALA LEU GLN VAL GLU LYS
SEQRES 6 A 484 SER GLY GLU GLU PHE GLU LEU SER VAL ASP LEU ILE LYS
SEQRES 7 A 484 ARG ILE HIS LYS LYS CYS GLY LYS LYS VAL GLU GLU LEU
SEQRES 8 A 484 GLN GLU LYS ASN PRO GLY GLU LEU ARG THR ASP GLU PRO
SEQRES 9 A 484 VAL SER PHE GLY ILE PRO ALA GLY ARG ALA SER ILE LYS
SEQRES 10 A 484 GLY ILE GLU GLU PHE LEU SER LEU VAL PHE LEU THR GLU
SEQRES 11 A 484 GLY GLY ALA GLU PHE GLY PRO GLY LYS ALA GLY PRO PHE
SEQRES 12 A 484 GLY PRO ARG PHE ASP LYS ASN TYR PHE LYS ASN LEU ASN
SEQRES 13 A 484 PRO GLU GLN ILE PRO ASP LEU ALA LYS GLN ILE TYR PHE
SEQRES 14 A 484 ASP MET CYS LYS TYR GLY HIS SER ASN THR ASN HIS PHE
SEQRES 15 A 484 TYR LEU ALA VAL MET LYS ASN VAL ASP VAL TYR LEU GLU
SEQRES 16 A 484 LYS ILE THR GLN SER TYR ASN LYS GLU ILE LYS THR ALA
SEQRES 17 A 484 GLU THR LEU ASP GLU LYS LEU LYS ILE ILE VAL LYS HIS
SEQRES 18 A 484 ILE ARG MET TYR GLU VAL LEU HIS PRO PHE ARG ASP ALA
SEQRES 19 A 484 ASN GLY ARG THR PHE VAL ASN ASN LEU LEU ASN ILE PRO
SEQRES 20 A 484 LEU MET GLN GLN GLY LEU PRO PRO ALA THR PHE TYR GLU
SEQRES 21 A 484 PRO ASN VAL PHE ASP LEU TYR SER ALA GLU GLU LEU VAL
SEQRES 22 A 484 VAL VAL VAL LYS GLU ALA ILE PHE ASN THR VAL GLU ILE
SEQRES 23 A 484 ILE GLU GLN SER LYS ARG LYS THR PRO ILE THR LEU TYR
SEQRES 24 A 484 GLY TYR HIS SER SER LEU GLU GLU GLN THR LYS PHE ARG
SEQRES 25 A 484 ASP MET LEU ASP SER PRO SER TYR GLU LYS ILE LYS HIS
SEQRES 26 A 484 MET ASP PHE SER ASP LEU ASN PRO GLU LYS LEU HIS LEU
SEQRES 27 A 484 LYS THR GLN LYS CYS LEU SER SER LEU ASN GLU GLN TYR
SEQRES 28 A 484 PRO LEU HIS ARG GLY ALA ILE TYR LEU SER ASP PRO GLY
SEQRES 29 A 484 GLU ILE LYS LEU LEU LEU SER ASN ARG ASN GLU SER GLN
SEQRES 30 A 484 ILE ASN GLN GLN ILE GLU GLN GLY ALA PRO PRO ILE TYR
SEQRES 31 A 484 VAL GLY LYS THR PRO ALA HIS LEU ALA VAL ILE SER GLY
SEQRES 32 A 484 ASN MET ALA MET LEU ASP GLU LEU ILE ALA LYS LYS ALA
SEQRES 33 A 484 ASP LEU SER LEU GLN ASP TYR ASP GLY LYS THR ALA LEU
SEQRES 34 A 484 HIS TYR ALA ALA GLU CYS GLY ASN MET GLN ILE MET GLY
SEQRES 35 A 484 LYS ILE LEU LYS VAL VAL LEU SER GLN GLU ASP ALA ILE
SEQRES 36 A 484 LYS VAL LEU ASN ILE LYS ASP ASN HIS GLY LYS THR ALA
SEQRES 37 A 484 PHE HIS TYR ALA ALA GLU PHE GLY THR PRO GLU LEU ILE
SEQRES 38 A 484 SER ALA LEU
HET C5P A1000 35
HET PC A2000 26
HET SO4 A3000 5
HET SO4 A3001 5
HET SO4 A3002 5
HETNAM C5P CYTIDINE-5'-MONOPHOSPHATE
HETNAM PC PHOSPHOCHOLINE
HETNAM SO4 SULFATE ION
FORMUL 2 C5P C9 H14 N3 O8 P
FORMUL 3 PC C5 H15 N O4 P 1+
FORMUL 4 SO4 3(O4 S 2-)
FORMUL 7 HOH *54(H2 O)
HELIX 1 1 GLY A 10 TYR A 17 1 8
HELIX 2 2 PRO A 18 PHE A 26 5 9
HELIX 3 3 TRP A 38 GLU A 45 1 8
HELIX 4 4 GLY A 47 LYS A 65 1 19
HELIX 5 5 SER A 73 GLY A 85 1 13
HELIX 6 6 PRO A 110 ARG A 113 5 4
HELIX 7 7 SER A 115 LEU A 125 1 11
HELIX 8 8 LEU A 125 GLY A 131 1 7
HELIX 9 9 GLN A 159 GLY A 175 1 17
HELIX 10 10 ASN A 189 ALA A 208 1 20
HELIX 11 11 THR A 210 LEU A 228 1 19
HELIX 12 12 ALA A 234 VAL A 240 1 7
HELIX 13 13 LEU A 244 GLN A 251 1 8
HELIX 14 14 SER A 268 ARG A 292 1 25
HELIX 15 15 THR A 297 TYR A 301 5 5
HELIX 16 16 SER A 304 LEU A 315 1 12
HELIX 17 17 SER A 317 HIS A 325 1 9
HELIX 18 18 ASN A 332 SER A 345 1 14
HELIX 19 19 SER A 346 ASN A 348 5 3
HELIX 20 20 TYR A 351 LEU A 360 1 10
HELIX 21 21 ASP A 362 SER A 371 1 10
HELIX 22 22 ASN A 374 ASN A 379 1 6
HELIX 23 23 THR A 394 GLY A 403 1 10
HELIX 24 24 ASN A 404 LYS A 414 1 11
HELIX 25 25 THR A 427 GLY A 436 1 10
HELIX 26 26 ASN A 437 SER A 450 1 14
HELIX 27 27 ASP A 453 ASN A 459 1 7
HELIX 28 28 THR A 467 GLU A 474 1 8
SHEET 1 AA 4 SER A 106 ILE A 109 0
SHEET 2 AA 4 HIS A 181 LEU A 184 -1 O HIS A 181 N ILE A 109
SHEET 3 AA 4 GLU A 134 GLY A 141 -1 O GLU A 134 N LEU A 184
SHEET 4 AA 4 GLY A 144 PHE A 147 -1 O GLY A 144 N GLY A 141
SITE 1 AC1 15 ASP A 28 ARG A 30 PHE A 31 TYR A 41
SITE 2 AC1 15 ARG A 44 CYS A 48 ALA A 234 ASN A 235
SITE 3 AC1 15 GLY A 236 ARG A 237 PRO A 261 ASN A 262
SITE 4 AC1 15 PC A2000 HOH A2030 SO4 A3002
SITE 1 AC2 11 PHE A 107 GLU A 226 HIS A 229 ASP A 233
SITE 2 AC2 11 ALA A 234 ASN A 235 ASN A 262 C5P A1000
SITE 3 AC2 11 HOH A2030 HOH A2034 SO4 A3002
SITE 1 AC3 6 SER A 124 LEU A 125 VAL A 126 PHE A 127
SITE 2 AC3 6 MET A 224 ILE A 481
SITE 1 AC4 5 PRO A 110 GLY A 112 ARG A 113 SER A 177
SITE 2 AC4 5 GLU A 260
SITE 1 AC5 6 ARG A 30 ARG A 113 ASN A 262 C5P A1000
SITE 2 AC5 6 PC A2000 HOH A2053
CRYST1 84.275 122.304 54.985 90.00 90.00 90.00 P 21 21 2 4
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 0.011866 0.000000 0.000000 0.00000
SCALE2 0.000000 0.008176 0.000000 0.00000
SCALE3 0.000000 0.000000 0.018187 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
