HEADER HYDROLASE 08-NOV-04 1XXV
TITLE YERSINIA YOPH (RESIDUES 163-468) BINDS PHOSPHONODIFLUOROMETHYL-PHE
TITLE 2 CONTAINING HEXAPEPTIDE AT TWO SITES
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROTEIN-TYROSINE PHOSPHATASE YOPH;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: CATALYTIC DOMAIN, RESIDUES 163-468;
COMPND 5 SYNONYM: VIRULENCE PROTEIN;
COMPND 6 EC: 3.1.3.48;
COMPND 7 ENGINEERED: YES;
COMPND 8 MUTATION: YES;
COMPND 9 MOL_ID: 2;
COMPND 10 MOLECULE: EPIDERMAL GROWTH FACTOR RECEPTOR DERIVED PEPTIDE;
COMPND 11 CHAIN: C, D, E, F;
COMPND 12 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: YERSINIA ENTEROCOLITICA;
SOURCE 3 ORGANISM_TAXID: 630;
SOURCE 4 GENE: YOPH, YOP51;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PT7-7;
SOURCE 10 MOL_ID: 2;
SOURCE 11 SYNTHETIC: YES;
SOURCE 12 OTHER_DETAILS: CHEMICALLY SYNTHESIZED BY ROBERT ZAMBONI AND MICHAEL
SOURCE 13 GRESSER, MERCK FROSST, MONTREAL
KEYWDS CATALYTIC DOMAIN, PHOSPHOTYROSINE-BINDING SITES, SUBSTRATE TARGETING,
KEYWDS 2 HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR M.I.IVANOV,J.A.STUCKEY,H.L.SCHUBERT,M.A.SAPER,J.B.BLISKA
REVDAT 4 03-APR-24 1XXV 1 SEQADV LINK
REVDAT 3 14-SEP-11 1XXV 1 ATOM HET HETATM LINK
REVDAT 3 2 1 SEQADV SEQRES SITE VERSN
REVDAT 2 24-FEB-09 1XXV 1 VERSN
REVDAT 1 22-MAR-05 1XXV 0
JRNL AUTH M.I.IVANOV,J.A.STUCKEY,H.L.SCHUBERT,M.A.SAPER,J.B.BLISKA
JRNL TITL TWO SUBSTRATE-TARGETING SITES IN THE YERSINIA PROTEIN
JRNL TITL 2 TYROSINE PHOSPHATASE CO-OPERATE TO PROMOTE BACTERIAL
JRNL TITL 3 VIRULENCE
JRNL REF MOL.MICROBIOL. V. 55 1346 2005
JRNL REFN ISSN 0950-382X
JRNL PMID 15720545
JRNL DOI 10.1111/J.1365-2958.2005.04477.X
REMARK 2
REMARK 2 RESOLUTION. 2.50 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 85.5
REMARK 3 NUMBER OF REFLECTIONS : 18319
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 SET) : 0.178
REMARK 3 FREE R VALUE : 0.229
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : 892
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 : NULL
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.50
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.55
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.2040
REMARK 3 BIN FREE R VALUE : 0.2980
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 38
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 : 4534
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 297
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 22.00
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 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM SIGMAA (A) : NULL
REMARK 3 LOW RESOLUTION CUTOFF (A) : NULL
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM C-V SIGMAA (A) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.007
REMARK 3 BOND ANGLES (DEGREES) : 1.183
REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL
REMARK 3 IMPROPER ANGLES (DEGREES) : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : ISOTROPIC
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : 2.138 ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : NULL
REMARK 3 KSOL : NULL
REMARK 3 BSOL : NULL
REMARK 3
REMARK 3 NCS MODEL : NULL
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: RESTRAINED B REFINEMENT
REMARK 4
REMARK 4 1XXV COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 23-NOV-04.
REMARK 100 THE DEPOSITION ID IS D_1000030892.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : 298
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU RU300
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : GRAPHITE
REMARK 200 OPTICS : MONOCHROMATOR
REMARK 200
REMARK 200 DETECTOR TYPE : AREA DETECTOR
REMARK 200 DETECTOR MANUFACTURER : UCSD MARK III
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : SDMS
REMARK 200 DATA SCALING SOFTWARE : SDMS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 18319
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.500
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 85.5
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : 0.07500
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MERLOT
REMARK 200 STARTING MODEL: YOPH (RESIDUES 163-468) WITH BOUND VO4 (NOT
REMARK 200 SUBMITTED TO PDB)
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 45.69
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.26
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 10 MG/ML PROTEIN, 0.5 MM
REMARK 280 PHOSPHONODIFLUORO-PHE-CONTAINING PEPTIDE IN 1 MM IMIDAZOLE.
REMARK 280 PRECIPITANT: 22% POLYETHYLENE GLYCOL (PEG) 4000, 8 MM MNCL2, 0.1%
REMARK 280 BETA-MERCAPTOETHANOL, 100 MM HEPES, PH 7.5, VAPOR DIFFUSION,
REMARK 280 HANGING DROP, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,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
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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: TRIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2160 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 12300 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -9.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, C, D
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
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2160 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 12300 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -12.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, E, F
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 PRO A 163
REMARK 465 ARG A 164
REMARK 465 GLU A 165
REMARK 465 ARG A 166
REMARK 465 PRO A 167
REMARK 465 HIS A 168
REMARK 465 THR A 169
REMARK 465 SER A 170
REMARK 465 GLY A 171
REMARK 465 HIS A 172
REMARK 465 HIS A 173
REMARK 465 GLY A 174
REMARK 465 ALA A 175
REMARK 465 GLY A 176
REMARK 465 GLU A 177
REMARK 465 ALA A 178
REMARK 465 ARG A 179
REMARK 465 ALA A 180
REMARK 465 THR A 181
REMARK 465 ALA A 182
REMARK 465 PRO A 183
REMARK 465 SER A 184
REMARK 465 THR A 185
REMARK 465 VAL A 186
REMARK 465 PRO B 163
REMARK 465 ARG B 164
REMARK 465 GLU B 165
REMARK 465 ARG B 166
REMARK 465 PRO B 167
REMARK 465 HIS B 168
REMARK 465 THR B 169
REMARK 465 SER B 170
REMARK 465 GLY B 171
REMARK 465 HIS B 172
REMARK 465 HIS B 173
REMARK 465 GLY B 174
REMARK 465 ALA B 175
REMARK 465 GLY B 176
REMARK 465 GLU B 177
REMARK 465 ALA B 178
REMARK 465 ARG B 179
REMARK 465 ALA B 180
REMARK 465 THR B 181
REMARK 465 ALA B 182
REMARK 465 PRO B 183
REMARK 465 SER B 184
REMARK 465 THR B 185
REMARK 465 VAL B 186
REMARK 465 ACE C 100
REMARK 465 ASP C 101
REMARK 465 ALA C 102
REMARK 465 ACE D 0
REMARK 465 ACE E 100
REMARK 465 ASP E 101
REMARK 465 ALA E 102
REMARK 465 ACE F 0
REMARK 480
REMARK 480 ZERO OCCUPANCY ATOM
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 480 M RES C SSEQI ATOMS
REMARK 480 ASP E 103 CB CG OD1 OD2
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 VAL A 281 141.76 -170.09
REMARK 500 THR A 318 -112.69 -107.71
REMARK 500 ASN A 353 41.72 -104.74
REMARK 500 CYS A 403 -114.13 -117.69
REMARK 500 ASN A 424 31.05 -92.04
REMARK 500 ARG A 440 -72.53 -135.78
REMARK 500 ASN A 441 149.93 -171.74
REMARK 500 VAL A 445 78.45 78.85
REMARK 500 GLN A 446 -71.51 -71.66
REMARK 500 VAL B 281 142.51 -170.08
REMARK 500 THR B 318 -112.35 -108.41
REMARK 500 ASN B 353 41.15 -104.43
REMARK 500 CYS B 403 -114.91 -119.10
REMARK 500 ASN B 424 30.17 -92.06
REMARK 500 ARG B 440 -73.73 -135.91
REMARK 500 VAL B 445 77.80 78.50
REMARK 500 GLN B 446 -72.15 -71.20
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR CHAIN C OF EPIDERMAL GROWTH
REMARK 800 FACTOR RECEPTOR DERIVED PEPTIDE
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR CHAIN D OF EPIDERMAL GROWTH
REMARK 800 FACTOR RECEPTOR DERIVED PEPTIDE
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR CHAIN E OF EPIDERMAL GROWTH
REMARK 800 FACTOR RECEPTOR DERIVED PEPTIDE
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR CHAIN F OF EPIDERMAL GROWTH
REMARK 800 FACTOR RECEPTOR DERIVED PEPTIDE
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1XXP RELATED DB: PDB
REMARK 900 COMPANION STRUCTURE OF YOPH (RESIDUES 163-468) C403S BOUND TO A
REMARK 900 PHOSPHOTYROSYL-CONTAINING HEXAPEPTIDE
REMARK 900 RELATED ID: 1QZ0 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE YERSINIA PESTIS PHOSPHATASE YOPH IN
REMARK 900 COMPLEX WITH A PHOSPHOTYROSYL MIMETIC-CONTAINING HEXAPEPTIDE
DBREF 1XXV A 163 468 UNP P15273 YOPH_YEREN 163 468
DBREF 1XXV B 163 468 UNP P15273 YOPH_YEREN 163 468
DBREF 1XXV C 101 106 PDB 1XXV 1XXV 101 106
DBREF 1XXV D 1 6 PDB 1XXV 1XXV 1 6
DBREF 1XXV E 101 106 PDB 1XXV 1XXV 101 106
DBREF 1XXV F 1 6 PDB 1XXV 1XXV 1 6
SEQADV 1XXV ARG A 235 UNP P15273 CYS 235 ENGINEERED MUTATION
SEQADV 1XXV ARG B 235 UNP P15273 CYS 235 ENGINEERED MUTATION
SEQRES 1 A 306 PRO ARG GLU ARG PRO HIS THR SER GLY HIS HIS GLY ALA
SEQRES 2 A 306 GLY GLU ALA ARG ALA THR ALA PRO SER THR VAL SER PRO
SEQRES 3 A 306 TYR GLY PRO GLU ALA ARG ALA GLU LEU SER SER ARG LEU
SEQRES 4 A 306 THR THR LEU ARG ASN THR LEU ALA PRO ALA THR ASN ASP
SEQRES 5 A 306 PRO ARG TYR LEU GLN ALA CYS GLY GLY GLU LYS LEU ASN
SEQRES 6 A 306 ARG PHE ARG ASP ILE GLN CYS ARG ARG GLN THR ALA VAL
SEQRES 7 A 306 ARG ALA ASP LEU ASN ALA ASN TYR ILE GLN VAL GLY ASN
SEQRES 8 A 306 THR ARG THR ILE ALA CYS GLN TYR PRO LEU GLN SER GLN
SEQRES 9 A 306 LEU GLU SER HIS PHE ARG MET LEU ALA GLU ASN ARG THR
SEQRES 10 A 306 PRO VAL LEU ALA VAL LEU ALA SER SER SER GLU ILE ALA
SEQRES 11 A 306 ASN GLN ARG PHE GLY MET PRO ASP TYR PHE ARG GLN SER
SEQRES 12 A 306 GLY THR TYR GLY SER ILE THR VAL GLU SER LYS MET THR
SEQRES 13 A 306 GLN GLN VAL GLY LEU GLY ASP GLY ILE MET ALA ASP MET
SEQRES 14 A 306 TYR THR LEU THR ILE ARG GLU ALA GLY GLN LYS THR ILE
SEQRES 15 A 306 SER VAL PRO VAL VAL HIS VAL GLY ASN TRP PRO ASP GLN
SEQRES 16 A 306 THR ALA VAL SER SER GLU VAL THR LYS ALA LEU ALA SER
SEQRES 17 A 306 LEU VAL ASP GLN THR ALA GLU THR LYS ARG ASN MET TYR
SEQRES 18 A 306 GLU SER LYS GLY SER SER ALA VAL ALA ASP ASP SER LYS
SEQRES 19 A 306 LEU ARG PRO VAL ILE HIS CYS ARG ALA GLY VAL GLY ARG
SEQRES 20 A 306 THR ALA GLN LEU ILE GLY ALA MET CYS MET ASN ASP SER
SEQRES 21 A 306 ARG ASN SER GLN LEU SER VAL GLU ASP MET VAL SER GLN
SEQRES 22 A 306 MET ARG VAL GLN ARG ASN GLY ILE MET VAL GLN LYS ASP
SEQRES 23 A 306 GLU GLN LEU ASP VAL LEU ILE LYS LEU ALA GLU GLY GLN
SEQRES 24 A 306 GLY ARG PRO LEU LEU ASN SER
SEQRES 1 B 306 PRO ARG GLU ARG PRO HIS THR SER GLY HIS HIS GLY ALA
SEQRES 2 B 306 GLY GLU ALA ARG ALA THR ALA PRO SER THR VAL SER PRO
SEQRES 3 B 306 TYR GLY PRO GLU ALA ARG ALA GLU LEU SER SER ARG LEU
SEQRES 4 B 306 THR THR LEU ARG ASN THR LEU ALA PRO ALA THR ASN ASP
SEQRES 5 B 306 PRO ARG TYR LEU GLN ALA CYS GLY GLY GLU LYS LEU ASN
SEQRES 6 B 306 ARG PHE ARG ASP ILE GLN CYS ARG ARG GLN THR ALA VAL
SEQRES 7 B 306 ARG ALA ASP LEU ASN ALA ASN TYR ILE GLN VAL GLY ASN
SEQRES 8 B 306 THR ARG THR ILE ALA CYS GLN TYR PRO LEU GLN SER GLN
SEQRES 9 B 306 LEU GLU SER HIS PHE ARG MET LEU ALA GLU ASN ARG THR
SEQRES 10 B 306 PRO VAL LEU ALA VAL LEU ALA SER SER SER GLU ILE ALA
SEQRES 11 B 306 ASN GLN ARG PHE GLY MET PRO ASP TYR PHE ARG GLN SER
SEQRES 12 B 306 GLY THR TYR GLY SER ILE THR VAL GLU SER LYS MET THR
SEQRES 13 B 306 GLN GLN VAL GLY LEU GLY ASP GLY ILE MET ALA ASP MET
SEQRES 14 B 306 TYR THR LEU THR ILE ARG GLU ALA GLY GLN LYS THR ILE
SEQRES 15 B 306 SER VAL PRO VAL VAL HIS VAL GLY ASN TRP PRO ASP GLN
SEQRES 16 B 306 THR ALA VAL SER SER GLU VAL THR LYS ALA LEU ALA SER
SEQRES 17 B 306 LEU VAL ASP GLN THR ALA GLU THR LYS ARG ASN MET TYR
SEQRES 18 B 306 GLU SER LYS GLY SER SER ALA VAL ALA ASP ASP SER LYS
SEQRES 19 B 306 LEU ARG PRO VAL ILE HIS CYS ARG ALA GLY VAL GLY ARG
SEQRES 20 B 306 THR ALA GLN LEU ILE GLY ALA MET CYS MET ASN ASP SER
SEQRES 21 B 306 ARG ASN SER GLN LEU SER VAL GLU ASP MET VAL SER GLN
SEQRES 22 B 306 MET ARG VAL GLN ARG ASN GLY ILE MET VAL GLN LYS ASP
SEQRES 23 B 306 GLU GLN LEU ASP VAL LEU ILE LYS LEU ALA GLU GLY GLN
SEQRES 24 B 306 GLY ARG PRO LEU LEU ASN SER
SEQRES 1 C 8 ACE ASP ALA ASP GLU FTY LEU NH2
SEQRES 1 D 8 ACE ASP ALA ASP GLU FTY LEU NH2
SEQRES 1 E 8 ACE ASP ALA ASP GLU FTY LEU NH2
SEQRES 1 F 8 ACE ASP ALA ASP GLU FTY LEU NH2
MODRES 1XXV FTY C 105 TYR DEOXY-DIFLUOROMETHELENE-PHOSPHOTYROSINE
MODRES 1XXV FTY D 5 TYR DEOXY-DIFLUOROMETHELENE-PHOSPHOTYROSINE
MODRES 1XXV FTY E 105 TYR DEOXY-DIFLUOROMETHELENE-PHOSPHOTYROSINE
MODRES 1XXV FTY F 5 TYR DEOXY-DIFLUOROMETHELENE-PHOSPHOTYROSINE
HET FTY C 105 18
HET NH2 C 107 1
HET FTY D 5 18
HET NH2 D 7 1
HET FTY E 105 18
HET NH2 E 107 1
HET FTY F 5 18
HET NH2 F 7 1
HETNAM FTY DEOXY-DIFLUOROMETHELENE-PHOSPHOTYROSINE
HETNAM NH2 AMINO GROUP
FORMUL 3 FTY 4(C10 H12 F2 N O5 P)
FORMUL 3 NH2 4(H2 N)
FORMUL 7 HOH *297(H2 O)
HELIX 1 1 GLY A 190 LEU A 208 1 19
HELIX 2 2 ARG A 235 ALA A 239 5 5
HELIX 3 3 LEU A 263 SER A 265 5 3
HELIX 4 4 GLN A 266 ASN A 277 1 12
HELIX 5 5 SER A 287 ASN A 293 1 7
HELIX 6 6 GLN A 294 GLY A 297 5 4
HELIX 7 7 SER A 361 LYS A 386 1 26
HELIX 8 8 GLY A 408 ASP A 421 1 14
HELIX 9 9 SER A 428 ARG A 440 1 13
HELIX 10 10 LYS A 447 GLN A 461 1 15
HELIX 11 11 GLY B 190 LEU B 208 1 19
HELIX 12 12 LEU B 263 SER B 265 5 3
HELIX 13 13 GLN B 266 ASN B 277 1 12
HELIX 14 14 SER B 287 ASN B 293 1 7
HELIX 15 15 GLN B 294 GLY B 297 5 4
HELIX 16 16 SER B 361 LYS B 386 1 26
HELIX 17 17 GLY B 408 ASP B 421 1 14
HELIX 18 18 SER B 428 ARG B 440 1 13
HELIX 19 19 LYS B 447 GLN B 461 1 15
SHEET 1 A 8 ALA A 246 VAL A 251 0
SHEET 2 A 8 THR A 254 CYS A 259 -1 O ALA A 258 N ASN A 247
SHEET 3 A 8 VAL A 400 HIS A 402 1 O ILE A 401 N ILE A 257
SHEET 4 A 8 LEU A 282 VAL A 284 1 N ALA A 283 O VAL A 400
SHEET 5 A 8 ILE A 344 VAL A 351 1 O VAL A 349 N LEU A 282
SHEET 6 A 8 ILE A 327 ARG A 337 -1 N ASP A 330 O HIS A 350
SHEET 7 A 8 ILE A 311 GLY A 324 -1 N THR A 312 O ARG A 337
SHEET 8 A 8 GLY A 306 TYR A 308 -1 N GLY A 306 O VAL A 313
SHEET 1 B 8 ALA B 246 VAL B 251 0
SHEET 2 B 8 THR B 254 CYS B 259 -1 O ALA B 258 N ASN B 247
SHEET 3 B 8 VAL B 400 HIS B 402 1 O ILE B 401 N ILE B 257
SHEET 4 B 8 LEU B 282 VAL B 284 1 N ALA B 283 O VAL B 400
SHEET 5 B 8 ILE B 344 VAL B 351 1 O VAL B 349 N LEU B 282
SHEET 6 B 8 ILE B 327 ARG B 337 -1 N ASP B 330 O HIS B 350
SHEET 7 B 8 ILE B 311 GLY B 324 -1 N THR B 318 O MET B 331
SHEET 8 B 8 GLY B 306 TYR B 308 -1 N GLY B 306 O VAL B 313
LINK C GLU C 104 N FTY C 105 1555 1555 1.33
LINK C FTY C 105 N LEU C 106 1555 1555 1.33
LINK C LEU C 106 N NH2 C 107 1555 1555 1.26
LINK C GLU D 4 N FTY D 5 1555 1555 1.33
LINK C FTY D 5 N LEU D 6 1555 1555 1.33
LINK C LEU D 6 N NH2 D 7 1555 1555 1.25
LINK C GLU E 104 N FTY E 105 1555 1555 1.33
LINK C FTY E 105 N LEU E 106 1555 1555 1.33
LINK C LEU E 106 N NH2 E 107 1555 1555 1.25
LINK C GLU F 4 N FTY F 5 1555 1555 1.32
LINK C FTY F 5 N LEU F 6 1555 1555 1.33
LINK C LEU F 6 N NH2 F 7 1555 1555 1.25
SITE 1 AC1 19 PHE A 229 ARG A 230 ASP A 231 ILE A 232
SITE 2 AC1 19 ASP A 356 GLN A 357 CYS A 403 ARG A 404
SITE 3 AC1 19 ALA A 405 GLY A 406 VAL A 407 GLY A 408
SITE 4 AC1 19 ARG A 409 GLN A 446 HOH A 632 HOH A 745
SITE 5 AC1 19 HOH B 705 NH2 C 107 HOH C 624
SITE 1 AC2 14 ARG A 278 ARG A 295 LYS A 342 THR A 343
SITE 2 AC2 14 MET A 382 LYS A 386 SER A 388 SER A 389
SITE 3 AC2 14 HOH A 774 SER B 468 NH2 D 7 HOH D 539
SITE 4 AC2 14 HOH D 540 HOH D 542
SITE 1 AC3 17 HOH A 749 PHE B 229 ARG B 230 ASP B 231
SITE 2 AC3 17 ILE B 232 ASP B 356 GLN B 357 CYS B 403
SITE 3 AC3 17 ARG B 404 ALA B 405 GLY B 406 VAL B 407
SITE 4 AC3 17 GLY B 408 ARG B 409 GLN B 446 NH2 E 107
SITE 5 AC3 17 HOH E 783
SITE 1 AC4 15 SER A 468 ARG B 278 ARG B 295 LYS B 342
SITE 2 AC4 15 THR B 343 ILE B 344 SER B 345 LYS B 386
SITE 3 AC4 15 SER B 388 SER B 389 HOH B 709 NH2 F 7
SITE 4 AC4 15 HOH F 642 HOH F 644 HOH F 818
CRYST1 54.130 47.170 71.820 104.45 115.05 89.97 P 1 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 0.018474 -0.000010 0.008978 0.00000
SCALE2 0.000000 0.021200 0.006069 0.00000
SCALE3 0.000000 0.000000 0.015987 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
