HEADER TRANSFERASE 16-NOV-18 6I7J
TITLE CRYSTAL STRUCTURE OF MONOMERIC FICD MUTANT L258D
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ADENOSINE MONOPHOSPHATE-PROTEIN TRANSFERASE FICD;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: AMPYLATOR FICD,DE-AMPYLASE FICD,FIC DOMAIN-CONTAINING
COMPND 5 PROTEIN,HUNTINGTIN YEAST PARTNER E,HUNTINGTIN-INTERACTING PROTEIN 13,
COMPND 6 HIP-13,HUNTINGTIN-INTERACTING PROTEIN E;
COMPND 7 EC: 2.7.7.-,3.1.4.-;
COMPND 8 ENGINEERED: YES;
COMPND 9 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: FICD, HIP13, HYPE, UNQ3041/PRO9857;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE 9 EXPRESSION_SYSTEM_VARIANT: T7 EXPRESS LYSY/IQ
KEYWDS FIC, AMPYLATION, UPR, BIP, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR L.A.PERERA,Y.YAN,R.J.READ,D.RON
REVDAT 4 24-JAN-24 6I7J 1 REMARK
REVDAT 3 13-NOV-19 6I7J 1 JRNL
REVDAT 2 02-OCT-19 6I7J 1 JRNL
REVDAT 1 25-SEP-19 6I7J 0
JRNL AUTH L.A.PERERA,C.RATO,Y.YAN,L.NEIDHARDT,S.H.MCLAUGHLIN,R.J.READ,
JRNL AUTH 2 S.PREISSLER,D.RON
JRNL TITL AN OLIGOMERIC STATE-DEPENDENT SWITCH IN THE ER ENZYME FICD
JRNL TITL 2 REGULATES AMPYLATION AND DEAMPYLATION OF BIP.
JRNL REF EMBO J. V. 38 02177 2019
JRNL REFN ESSN 1460-2075
JRNL PMID 31531998
JRNL DOI 10.15252/EMBJ.2019102177
REMARK 2
REMARK 2 RESOLUTION. 2.65 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0238
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.65
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 62.80
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.5
REMARK 3 NUMBER OF REFLECTIONS : 17947
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) : 0.231
REMARK 3 R VALUE (WORKING SET) : 0.228
REMARK 3 FREE R VALUE : 0.283
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.900
REMARK 3 FREE R VALUE TEST SET COUNT : 919
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.65
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.72
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1267
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 97.82
REMARK 3 BIN R VALUE (WORKING SET) : 0.3550
REMARK 3 BIN FREE R VALUE SET COUNT : 76
REMARK 3 BIN FREE R VALUE : 0.3830
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2693
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 159
REMARK 3 SOLVENT ATOMS : 70
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 50.93
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 1.07000
REMARK 3 B22 (A**2) : 1.07000
REMARK 3 B33 (A**2) : -3.46000
REMARK 3 B12 (A**2) : 0.53000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.427
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.310
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.269
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 14.030
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.928
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.896
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2924 ; 0.003 ; 0.013
REMARK 3 BOND LENGTHS OTHERS (A): 2746 ; 0.001 ; 0.017
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3919 ; 1.222 ; 1.659
REMARK 3 BOND ANGLES OTHERS (DEGREES): 6365 ; 1.118 ; 1.601
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 342 ; 5.954 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 157 ;31.417 ;21.401
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 487 ;15.632 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 23 ;14.250 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 372 ; 0.049 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 3120 ; 0.003 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 597 ; 0.001 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 1362 ; 2.191 ; 5.272
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 1361 ; 2.191 ; 5.268
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 1706 ; 3.549 ; 7.898
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 1707 ; 3.548 ; 7.904
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1562 ; 2.270 ; 5.722
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 1563 ; 2.269 ; 5.725
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 2214 ; 3.812 ; 8.396
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 3134 ; 7.109 ;61.800
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 3135 ; 7.108 ;61.825
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 6I7J COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 16-NOV-18.
REMARK 100 THE DEPOSITION ID IS D_1200012925.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 27-NOV-17
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : DIAMOND
REMARK 200 BEAMLINE : I04
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97942
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M-F
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XIA2
REMARK 200 DATA SCALING SOFTWARE : AIMLESS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 18963
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.650
REMARK 200 RESOLUTION RANGE LOW (A) : 62.800
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 9.700
REMARK 200 R MERGE (I) : 0.17600
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 8.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.65
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.72
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 10.00
REMARK 200 R MERGE FOR SHELL (I) : 0.85600
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.200
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: 4U0U
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 69.77
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.07
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M TRIS PH 8.5; 2.0 M AMMONIUM
REMARK 280 SULPHATE, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31 2 1
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 Y,X,-Z
REMARK 290 5555 X-Y,-Y,-Z+2/3
REMARK 290 6555 -X,-X+Y,-Z+1/3
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 26.54600
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 53.09200
REMARK 290 SMTRY1 4 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 4 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 5 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 53.09200
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 26.54600
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: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 5380 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 17460 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -77.0 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 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 LEU A 440
REMARK 465 PRO A 441
REMARK 465 GLU A 442
REMARK 465 ALA A 443
REMARK 465 GLN A 444
REMARK 465 PRO A 445
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 SER A 103 OG
REMARK 470 LEU A 104 CG CD1 CD2
REMARK 470 LYS A 124 CG CD CE NZ
REMARK 470 LYS A 210 CG CD CE NZ
REMARK 470 TYR A 251 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 GLU A 341 CG CD OE1 OE2
REMARK 470 ASN A 345 CG OD1 ND2
REMARK 470 THR A 372 CG2
REMARK 470 TYR A 436 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 VAL A 438 CG1 CG2
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 HIS A 173 97.17 -61.43
REMARK 500 SER A 437 138.57 -170.57
REMARK 500
REMARK 500 REMARK: NULL
REMARK 610
REMARK 610 MISSING HETEROATOM
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 610 I=INSERTION CODE):
REMARK 610 M RES C SSEQI
REMARK 610 1PE A 509
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 503
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 504
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 505
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 506
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 507
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 1PE A 508
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 1PE A 509
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 1PE A 510
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PG4 A 511
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PG4 A 512
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PG4 A 513
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG A 514
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG A 515
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PG4 A 516
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PG4 A 517
DBREF 6I7J A 104 445 UNP Q9BVA6 FICD_HUMAN 104 445
SEQADV 6I7J SER A 103 UNP Q9BVA6 EXPRESSION TAG
SEQADV 6I7J ASP A 258 UNP Q9BVA6 LEU 258 ENGINEERED MUTATION
SEQRES 1 A 343 SER LEU GLU ALA ARG ALA ALA LEU ASN GLN ALA LEU GLU
SEQRES 2 A 343 MET LYS ARG GLN GLY LYS ARG GLU LYS ALA GLN LYS LEU
SEQRES 3 A 343 PHE MET HIS ALA LEU LYS MET ASP PRO ASP PHE VAL ASP
SEQRES 4 A 343 ALA LEU THR GLU PHE GLY ILE PHE SER GLU GLU ASP LYS
SEQRES 5 A 343 ASP ILE ILE GLN ALA ASP TYR LEU TYR THR ARG ALA LEU
SEQRES 6 A 343 THR ILE SER PRO TYR HIS GLU LYS ALA LEU VAL ASN ARG
SEQRES 7 A 343 ASP ARG THR LEU PRO LEU VAL GLU GLU ILE ASP GLN ARG
SEQRES 8 A 343 TYR PHE SER ILE ILE ASP SER LYS VAL LYS LYS VAL MET
SEQRES 9 A 343 SER ILE PRO LYS GLY ASN SER ALA LEU ARG ARG VAL MET
SEQRES 10 A 343 GLU GLU THR TYR TYR HIS HIS ILE TYR HIS THR VAL ALA
SEQRES 11 A 343 ILE GLU GLY ASN THR LEU THR LEU SER GLU ILE ARG HIS
SEQRES 12 A 343 ILE LEU GLU THR ARG TYR ALA VAL PRO GLY LYS SER ASP
SEQRES 13 A 343 GLU GLU GLN ASN GLU VAL ILE GLY MET HIS ALA ALA MET
SEQRES 14 A 343 LYS TYR ILE ASN THR THR LEU VAL SER ARG ILE GLY SER
SEQRES 15 A 343 VAL THR ILE SER ASP VAL LEU GLU ILE HIS ARG ARG VAL
SEQRES 16 A 343 LEU GLY TYR VAL ASP PRO VAL GLU ALA GLY ARG PHE ARG
SEQRES 17 A 343 THR THR GLN VAL LEU VAL GLY HIS HIS ILE PRO PRO HIS
SEQRES 18 A 343 PRO GLN ASP VAL GLU LYS GLN MET GLN GLU PHE VAL GLN
SEQRES 19 A 343 TRP LEU ASN SER GLU GLU ALA MET ASN LEU HIS PRO VAL
SEQRES 20 A 343 GLU PHE ALA ALA LEU ALA HIS TYR LYS LEU VAL TYR ILE
SEQRES 21 A 343 HIS PRO PHE ILE ASP GLY ASN GLY ARG THR SER ARG LEU
SEQRES 22 A 343 LEU MET ASN LEU ILE LEU MET GLN ALA GLY TYR PRO PRO
SEQRES 23 A 343 ILE THR ILE ARG LYS GLU GLN ARG SER ASP TYR TYR HIS
SEQRES 24 A 343 VAL LEU GLU ALA ALA ASN GLU GLY ASP VAL ARG PRO PHE
SEQRES 25 A 343 ILE ARG PHE ILE ALA LYS CYS THR GLU THR THR LEU ASP
SEQRES 26 A 343 THR LEU LEU PHE ALA THR THR GLU TYR SER VAL ALA LEU
SEQRES 27 A 343 PRO GLU ALA GLN PRO
HET SO4 A 501 5
HET SO4 A 502 5
HET SO4 A 503 5
HET SO4 A 504 5
HET SO4 A 505 5
HET SO4 A 506 5
HET SO4 A 507 5
HET 1PE A 508 16
HET 1PE A 509 13
HET 1PE A 510 16
HET PG4 A 511 13
HET PG4 A 512 13
HET PG4 A 513 13
HET PEG A 514 7
HET PEG A 515 7
HET PG4 A 516 13
HET PG4 A 517 13
HETNAM SO4 SULFATE ION
HETNAM 1PE PENTAETHYLENE GLYCOL
HETNAM PG4 TETRAETHYLENE GLYCOL
HETNAM PEG DI(HYDROXYETHYL)ETHER
HETSYN 1PE PEG400
FORMUL 2 SO4 7(O4 S 2-)
FORMUL 9 1PE 3(C10 H22 O6)
FORMUL 12 PG4 5(C8 H18 O5)
FORMUL 15 PEG 2(C4 H10 O3)
FORMUL 19 HOH *70(H2 O)
HELIX 1 AA1 ALA A 106 GLY A 120 1 15
HELIX 2 AA2 LYS A 121 ASP A 136 1 16
HELIX 3 AA3 PHE A 139 ASP A 153 1 15
HELIX 4 AA4 ASP A 155 SER A 170 1 16
HELIX 5 AA5 HIS A 173 MET A 206 1 34
HELIX 6 AA6 ASN A 212 ILE A 233 1 22
HELIX 7 AA7 THR A 239 THR A 249 1 11
HELIX 8 AA8 SER A 257 THR A 277 1 21
HELIX 9 AA9 THR A 286 GLY A 299 1 14
HELIX 10 AB1 HIS A 323 ASN A 339 1 17
HELIX 11 AB2 SER A 340 LEU A 346 1 7
HELIX 12 AB3 HIS A 347 HIS A 363 1 17
HELIX 13 AB4 GLY A 368 ALA A 384 1 17
HELIX 14 AB5 ARG A 392 GLU A 394 5 3
HELIX 15 AB6 GLN A 395 GLU A 408 1 14
HELIX 16 AB7 VAL A 411 PHE A 431 1 21
SITE 1 AC1 7 ARG A 217 HIS A 363 GLY A 368 ASN A 369
SITE 2 AC1 7 GLY A 370 SO4 A 506 HOH A 612
SITE 1 AC2 4 THR A 239 SER A 241 TYR A 400 HOH A 622
SITE 1 AC3 6 GLN A 112 ARG A 295 GLY A 299 TYR A 300
SITE 2 AC3 6 HOH A 611 HOH A 619
SITE 1 AC4 3 LYS A 203 TYR A 386 HOH A 607
SITE 1 AC5 5 SER A 241 HIS A 245 SER A 397 TYR A 400
SITE 2 AC5 5 HIS A 401
SITE 1 AC6 5 GLY A 370 TYR A 399 SO4 A 501 PG4 A 513
SITE 2 AC6 5 HOH A 620
SITE 1 AC7 3 ARG A 396 TYR A 400 PG4 A 513
SITE 1 AC8 4 TRP A 337 TYR A 357 LYS A 358 PG4 A 512
SITE 1 AC9 3 MET A 219 TYR A 224 HOH A 633
SITE 1 AD1 4 ILE A 320 ARG A 392 ASP A 427 PEG A 515
SITE 1 AD2 2 TYR A 161 HOH A 642
SITE 1 AD3 6 TYR A 357 LYS A 358 TYR A 361 ALA A 406
SITE 2 AD3 6 GLY A 409 1PE A 508
SITE 1 AD4 7 HIS A 319 TYR A 361 TYR A 400 GLU A 404
SITE 2 AD4 7 ASN A 407 SO4 A 506 SO4 A 507
SITE 1 AD5 4 ALA A 109 GLN A 112 MET A 135 TYR A 300
SITE 1 AD6 1 1PE A 510
SITE 1 AD7 6 VAL A 205 MET A 206 ILE A 208 LEU A 215
SITE 2 AD7 6 MET A 219 TYR A 386
SITE 1 AD8 5 GLY A 120 LYS A 121 ARG A 122 GLU A 123
SITE 2 AD8 5 LYS A 124
CRYST1 118.099 118.099 79.638 90.00 90.00 120.00 P 31 2 1 6
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 0.008467 0.004889 0.000000 0.00000
SCALE2 0.000000 0.009777 0.000000 0.00000
SCALE3 0.000000 0.000000 0.012557 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
