HEADER LIGASE 19-FEB-08 2ZIO
TITLE CRYSTAL STRUCTURE OF THE CATALYTIC DOMAIN OF PYRROLYSYL-TRNA
TITLE 2 SYNTHETASE IN COMPLEX WITH ALOCLYS-AMP AND PNP
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PYRROLYSYL-TRNA SYNTHETASE;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: C-TERMINAL FRAGMENT;
COMPND 5 SYNONYM: PYRROLYSINE--TRNA LIGASE, PYLRS;
COMPND 6 EC: 6.1.1.26;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: METHANOSARCINA MAZEI;
SOURCE 3 ORGANISM_TAXID: 2209;
SOURCE 4 STRAIN: JCM9314;
SOURCE 5 GENE: PYLS;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3) CODON PLUS;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET28C
KEYWDS AMINOACYL-TRNA SYNTHETASE, PYRROLYSYL-TRNA SYNTHETASE, TRNA,
KEYWDS 2 PYRROLYSINE, ATP ANALOGUE, NON-NATURAL AMINO ACID, UNNATURAL AMINO
KEYWDS 3 ACID, ATP-BINDING, CYTOPLASM, LIGASE, NUCLEOTIDE-BINDING, PROTEIN
KEYWDS 4 BIOSYNTHESIS, STRUCTURAL GENOMICS, NPPSFA, NATIONAL PROJECT ON
KEYWDS 5 PROTEIN STRUCTURAL AND FUNCTIONAL ANALYSES, RIKEN STRUCTURAL
KEYWDS 6 GENOMICS/PROTEOMICS INITIATIVE, RSGI
EXPDTA X-RAY DIFFRACTION
AUTHOR T.YANAGISAWA,R.ISHII,S.YOKOYAMA,RIKEN STRUCTURAL GENOMICS/PROTEOMICS
AUTHOR 2 INITIATIVE (RSGI)
REVDAT 3 01-NOV-23 2ZIO 1 REMARK SEQADV
REVDAT 2 09-DEC-08 2ZIO 1 REMARK
REVDAT 1 02-DEC-08 2ZIO 0
JRNL AUTH T.YANAGISAWA,R.ISHII,R.FUKUNAGA,T.KOBAYASHI,K.SAKAMOTO,
JRNL AUTH 2 S.YOKOYAMA
JRNL TITL MULTISTEP ENGINEERING OF PYRROLYSYL-TRNA SYNTHETASE TO
JRNL TITL 2 GENETICALLY ENCODE N(VAREPSILON)-(O-AZIDOBENZYLOXYCARBONYL)
JRNL TITL 3 LYSINE FOR SITE-SPECIFIC PROTEIN MODIFICATION
JRNL REF CHEM.BIOL. V. 15 1187 2008
JRNL REFN ISSN 1074-5521
JRNL PMID 19022179
JRNL DOI 10.1016/J.CHEMBIOL.2008.10.004
REMARK 2
REMARK 2 RESOLUTION. 2.06 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.1
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 : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.06
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 42.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 1664781.090
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 99.2
REMARK 3 NUMBER OF REFLECTIONS : 26965
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) : 0.183
REMARK 3 FREE R VALUE : 0.213
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 9.900
REMARK 3 FREE R VALUE TEST SET COUNT : 2681
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.004
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 6
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.06
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.19
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 94.30
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 3816
REMARK 3 BIN R VALUE (WORKING SET) : 0.2640
REMARK 3 BIN FREE R VALUE : 0.3080
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 10.20
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 433
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.015
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2074
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 47
REMARK 3 SOLVENT ATOMS : 152
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 29.30
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 52.20
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -3.84000
REMARK 3 B22 (A**2) : -3.84000
REMARK 3 B33 (A**2) : 7.67000
REMARK 3 B12 (A**2) : 0.47000
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) : 0.21
REMARK 3 ESD FROM SIGMAA (A) : 0.26
REMARK 3 LOW RESOLUTION CUTOFF (A) : 5.00
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.26
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.32
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.009
REMARK 3 BOND ANGLES (DEGREES) : 1.500
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 23.40
REMARK 3 IMPROPER ANGLES (DEGREES) : 2.080
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : RESTRAINED
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : 4.700 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 6.370 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 7.310 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 9.520 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.36
REMARK 3 BSOL : 61.35
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 : PROTEIN_REP.PARAM
REMARK 3 PARAMETER FILE 2 : WATER_REP.PARAM
REMARK 3 PARAMETER FILE 3 : ION.PARAM
REMARK 3 PARAMETER FILE 4 : LIGAND5.PARAM
REMARK 3 PARAMETER FILE 5 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : WATER.TOP
REMARK 3 TOPOLOGY FILE 3 : ION.TOP
REMARK 3 TOPOLOGY FILE 4 : LIGAND5.TOP
REMARK 3 TOPOLOGY FILE 5 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2ZIO COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 21-FEB-08.
REMARK 100 THE DEPOSITION ID IS D_1000028020.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 25-JUL-05
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SPRING-8
REMARK 200 BEAMLINE : BL41XU
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0000
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 26977
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.060
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.9
REMARK 200 DATA REDUNDANCY : 8.500
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.05900
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) : 2.06
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.10
REMARK 200 COMPLETENESS FOR SHELL (%) : 82.4
REMARK 200 DATA REDUNDANCY IN SHELL : 4.70
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.33900
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: MOLREP
REMARK 200 STARTING MODEL: 1WK3
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 63.14
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.34
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NA/CACODYLATE, MGCL2, PEG3350, PH 7.0,
REMARK 280 VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 64
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
REMARK 290 5555 Y,-X+Y,Z+1/3
REMARK 290 6555 X-Y,X,Z+2/3
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 23.68667
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 47.37333
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 0.00000
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 23.68667
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 47.37333
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: 5340 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 23030 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -18.8 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 52.07500
REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 90.19655
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 MET A -21
REMARK 465 GLY A -20
REMARK 465 SER A -19
REMARK 465 SER A -18
REMARK 465 HIS A -17
REMARK 465 HIS A -16
REMARK 465 HIS A -15
REMARK 465 HIS A -14
REMARK 465 HIS A -13
REMARK 465 HIS A -12
REMARK 465 SER A -11
REMARK 465 SER A -10
REMARK 465 GLY A -9
REMARK 465 LEU A -8
REMARK 465 VAL A -7
REMARK 465 PRO A -6
REMARK 465 ARG A -5
REMARK 465 GLY A -4
REMARK 465 SER A -3
REMARK 465 HIS A -2
REMARK 465 MET A -1
REMARK 465 ALA A 185
REMARK 465 SER A 186
REMARK 465 ALA A 187
REMARK 465 ILE A 208
REMARK 465 SER A 209
REMARK 465 LEU A 210
REMARK 465 ASN A 211
REMARK 465 ASP A 281
REMARK 465 THR A 282
REMARK 465 GLU A 283
REMARK 465 LYS A 336
REMARK 465 SER A 380
REMARK 465 CYS A 381
REMARK 465 MET A 382
REMARK 465 VAL A 383
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 214 144.80 -31.85
REMARK 500 GLU A 237 -95.67 -107.24
REMARK 500 GLU A 238 -81.86 -44.23
REMARK 500 ARG A 239 2.80 83.68
REMARK 500 ASP A 292 -156.41 55.38
REMARK 500 SER A 333 -62.86 -130.48
REMARK 500 ASP A 334 -158.21 -71.27
REMARK 500 ASN A 453 74.10 -104.04
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 RESIDUE 2PN A 1
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AYB A 601
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2E3C RELATED DB: PDB
REMARK 900 LIGAND-FREE FORM
REMARK 900 RELATED ID: 2ZCD RELATED DB: PDB
REMARK 900 AMPPNP-BOUND FORM
REMARK 900 RELATED ID: 2ZCE RELATED DB: PDB
REMARK 900 PYRROLYSINE/AMPPNP-BOUND FORM
REMARK 900 RELATED ID: 2ZIN RELATED DB: PDB
REMARK 900 BOC-LYS/AMPPNP-BOUND FORM
REMARK 900 RELATED ID: TRT00100322.6 RELATED DB: TARGETDB
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 THIS CONFLICT IS DUE TO THE STRAIN DIFFERENCE
REMARK 999 (JCM9314 AND GOE1).
DBREF 2ZIO A 185 454 UNP Q8PWY1 PYLS_METMA 185 454
SEQADV 2ZIO MET A -21 UNP Q8PWY1 EXPRESSION TAG
SEQADV 2ZIO GLY A -20 UNP Q8PWY1 EXPRESSION TAG
SEQADV 2ZIO SER A -19 UNP Q8PWY1 EXPRESSION TAG
SEQADV 2ZIO SER A -18 UNP Q8PWY1 EXPRESSION TAG
SEQADV 2ZIO HIS A -17 UNP Q8PWY1 EXPRESSION TAG
SEQADV 2ZIO HIS A -16 UNP Q8PWY1 EXPRESSION TAG
SEQADV 2ZIO HIS A -15 UNP Q8PWY1 EXPRESSION TAG
SEQADV 2ZIO HIS A -14 UNP Q8PWY1 EXPRESSION TAG
SEQADV 2ZIO HIS A -13 UNP Q8PWY1 EXPRESSION TAG
SEQADV 2ZIO HIS A -12 UNP Q8PWY1 EXPRESSION TAG
SEQADV 2ZIO SER A -11 UNP Q8PWY1 EXPRESSION TAG
SEQADV 2ZIO SER A -10 UNP Q8PWY1 EXPRESSION TAG
SEQADV 2ZIO GLY A -9 UNP Q8PWY1 EXPRESSION TAG
SEQADV 2ZIO LEU A -8 UNP Q8PWY1 EXPRESSION TAG
SEQADV 2ZIO VAL A -7 UNP Q8PWY1 EXPRESSION TAG
SEQADV 2ZIO PRO A -6 UNP Q8PWY1 EXPRESSION TAG
SEQADV 2ZIO ARG A -5 UNP Q8PWY1 EXPRESSION TAG
SEQADV 2ZIO GLY A -4 UNP Q8PWY1 EXPRESSION TAG
SEQADV 2ZIO SER A -3 UNP Q8PWY1 EXPRESSION TAG
SEQADV 2ZIO HIS A -2 UNP Q8PWY1 EXPRESSION TAG
SEQADV 2ZIO MET A -1 UNP Q8PWY1 EXPRESSION TAG
SEQADV 2ZIO GLY A 444 UNP Q8PWY1 GLU 444 SEE REMARK 999
SEQRES 1 A 291 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 A 291 LEU VAL PRO ARG GLY SER HIS MET ALA SER ALA PRO ALA
SEQRES 3 A 291 LEU THR LYS SER GLN THR ASP ARG LEU GLU VAL LEU LEU
SEQRES 4 A 291 ASN PRO LYS ASP GLU ILE SER LEU ASN SER GLY LYS PRO
SEQRES 5 A 291 PHE ARG GLU LEU GLU SER GLU LEU LEU SER ARG ARG LYS
SEQRES 6 A 291 LYS ASP LEU GLN GLN ILE TYR ALA GLU GLU ARG GLU ASN
SEQRES 7 A 291 TYR LEU GLY LYS LEU GLU ARG GLU ILE THR ARG PHE PHE
SEQRES 8 A 291 VAL ASP ARG GLY PHE LEU GLU ILE LYS SER PRO ILE LEU
SEQRES 9 A 291 ILE PRO LEU GLU TYR ILE GLU ARG MET GLY ILE ASP ASN
SEQRES 10 A 291 ASP THR GLU LEU SER LYS GLN ILE PHE ARG VAL ASP LYS
SEQRES 11 A 291 ASN PHE CYS LEU ARG PRO MET LEU ALA PRO ASN LEU TYR
SEQRES 12 A 291 ASN TYR LEU ARG LYS LEU ASP ARG ALA LEU PRO ASP PRO
SEQRES 13 A 291 ILE LYS ILE PHE GLU ILE GLY PRO CYS TYR ARG LYS GLU
SEQRES 14 A 291 SER ASP GLY LYS GLU HIS LEU GLU GLU PHE THR MET LEU
SEQRES 15 A 291 ASN PHE CYS GLN MET GLY SER GLY CYS THR ARG GLU ASN
SEQRES 16 A 291 LEU GLU SER ILE ILE THR ASP PHE LEU ASN HIS LEU GLY
SEQRES 17 A 291 ILE ASP PHE LYS ILE VAL GLY ASP SER CYS MET VAL TYR
SEQRES 18 A 291 GLY ASP THR LEU ASP VAL MET HIS GLY ASP LEU GLU LEU
SEQRES 19 A 291 SER SER ALA VAL VAL GLY PRO ILE PRO LEU ASP ARG GLU
SEQRES 20 A 291 TRP GLY ILE ASP LYS PRO TRP ILE GLY ALA GLY PHE GLY
SEQRES 21 A 291 LEU GLU ARG LEU LEU LYS VAL LYS HIS ASP PHE LYS ASN
SEQRES 22 A 291 ILE LYS ARG ALA ALA ARG SER GLY SER TYR TYR ASN GLY
SEQRES 23 A 291 ILE SER THR ASN LEU
HET 2PN A 1 9
HET AYB A 601 38
HETNAM 2PN IMIDODIPHOSPHORIC ACID
HETNAM AYB 5'-O-[(S)-({(2S)-2-AMINO-6-[(PROPOXYCARBONYL)
HETNAM 2 AYB AMINO]HEXANOYL}OXY)(HYDROXY)PHOSPHORYL]ADENOSINE
HETSYN AYB NE-ALLYLOXYCARBONYL-L-LYSINE-5'-ADENOSINE MONOPHOSPHATE
FORMUL 2 2PN H5 N O6 P2
FORMUL 3 AYB C20 H32 N7 O10 P
FORMUL 4 HOH *152(H2 O)
HELIX 1 1 THR A 191 LEU A 202 1 12
HELIX 2 2 PRO A 215 GLU A 237 1 23
HELIX 3 3 ASN A 241 ARG A 257 1 17
HELIX 4 4 LEU A 270 ARG A 275 1 6
HELIX 5 5 LEU A 301 ASP A 313 1 13
HELIX 6 6 THR A 355 GLY A 371 1 17
HELIX 7 7 ILE A 405 GLY A 412 5 8
HELIX 8 8 LEU A 424 ASP A 433 1 10
HELIX 9 9 ASN A 436 ALA A 440 5 5
SHEET 1 A 7 LEU A 260 ILE A 262 0
SHEET 2 A 7 ILE A 320 TYR A 329 1 O PHE A 323 N ILE A 262
SHEET 3 A 7 GLU A 341 MET A 350 -1 O CYS A 348 N ILE A 322
SHEET 4 A 7 TRP A 417 GLY A 423 -1 O PHE A 422 N LEU A 345
SHEET 5 A 7 LEU A 395 VAL A 402 -1 N VAL A 401 O GLY A 419
SHEET 6 A 7 THR A 387 HIS A 392 -1 N VAL A 390 O SER A 398
SHEET 7 A 7 LYS A 375 VAL A 377 -1 N LYS A 375 O MET A 391
SHEET 1 B 3 LEU A 267 PRO A 269 0
SHEET 2 B 3 PHE A 295 LEU A 297 -1 O CYS A 296 N ILE A 268
SHEET 3 B 3 ARG A 290 VAL A 291 -1 N VAL A 291 O PHE A 295
SHEET 1 C 2 TYR A 446 TYR A 447 0
SHEET 2 C 2 ILE A 450 SER A 451 -1 O ILE A 450 N TYR A 447
CISPEP 1 ASP A 318 PRO A 319 0 -0.04
CISPEP 2 GLY A 403 PRO A 404 0 -0.08
SITE 1 AC1 5 HIS A 338 LEU A 395 GLU A 396 ARG A 426
SITE 2 AC1 5 HOH A 753
SITE 1 AC2 25 ALA A 302 LEU A 309 ARG A 330 GLU A 332
SITE 2 AC2 25 GLU A 337 LEU A 339 PHE A 342 MET A 344
SITE 3 AC2 25 ASN A 346 GLU A 396 LEU A 397 SER A 398
SITE 4 AC2 25 SER A 399 TRP A 417 ALA A 420 GLY A 421
SITE 5 AC2 25 GLY A 423 ARG A 426 HOH A 604 HOH A 608
SITE 6 AC2 25 HOH A 637 HOH A 640 HOH A 684 HOH A 705
SITE 7 AC2 25 HOH A 753
CRYST1 104.150 104.150 71.060 90.00 90.00 120.00 P 64 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 0.009602 0.005543 0.000000 0.00000
SCALE2 0.000000 0.011087 0.000000 0.00000
SCALE3 0.000000 0.000000 0.014073 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
