HEADER LIGASE 30-AUG-06 2DXT
TITLE CRYSTAL STRUCTURE OF BIOTIN PROTEIN LIGASE FROM PYROCOCCUS HORIKOSHII
TITLE 2 COMPLEXED WITH ATP AND BIOTIN, MUTATION D104A
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: BIOTIN--[ACETYL-COA-CARBOXYLASE] LIGASE;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: BIOTIN PROTEIN LIGASE;
COMPND 5 EC: 6.3.4.15;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: PYROCOCCUS HORIKOSHII;
SOURCE 3 ORGANISM_TAXID: 53953;
SOURCE 4 GENE: BIRA;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: (DE3)RIL;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET 11A
KEYWDS BIOTIN BIOSYNTHESIS, DIMER, STRUCTURAL GENOMICS, NPPSFA, NATIONAL
KEYWDS 2 PROJECT ON PROTEIN STRUCTURAL AND FUNCTIONAL ANALYSES, RIKEN
KEYWDS 3 STRUCTURAL GENOMICS/PROTEOMICS INITIATIVE, RSGI, LIGASE
EXPDTA X-RAY DIFFRACTION
AUTHOR B.BAGAUTDINOV,Y.MATSUURA,N.KUNISHIMA,RIKEN STRUCTURAL
AUTHOR 2 GENOMICS/PROTEOMICS INITIATIVE (RSGI)
REVDAT 4 25-OCT-23 2DXT 1 REMARK
REVDAT 3 10-NOV-21 2DXT 1 REMARK SEQADV
REVDAT 2 24-FEB-09 2DXT 1 VERSN
REVDAT 1 01-MAR-07 2DXT 0
JRNL AUTH B.BAGAUTDINOV,Y.MATSUURA,N.KUNISHIMA
JRNL TITL LIGAND STRUCTURES OF BIOTIN PROTEIN LIGASE FROM PYROCOCCUS
JRNL TITL 2 HORIKOSHII OT3
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.60 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 : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.60
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 37.23
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) (%) : 90.8
REMARK 3 NUMBER OF REFLECTIONS : 51912
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) : 0.188
REMARK 3 FREE R VALUE : 0.201
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : 2572
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) : NULL
REMARK 3 BIN RESOLUTION RANGE LOW (A) : NULL
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : NULL
REMARK 3 BIN FREE R VALUE : NULL
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : NULL
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 : 3668
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 94
REMARK 3 SOLVENT ATOMS : 564
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 21.24
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 25.90
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -1.05000
REMARK 3 B22 (A**2) : -6.61000
REMARK 3 B33 (A**2) : 7.66000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 2.02000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.18
REMARK 3 ESD FROM SIGMAA (A) : 0.17
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) : 0.20
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.18
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.007
REMARK 3 BOND ANGLES (DEGREES) : 1.300
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 23.80
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.890
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : OVERALL
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) : NULL ; 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: NULL
REMARK 4
REMARK 4 2DXT COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 01-SEP-06.
REMARK 100 THE DEPOSITION ID IS D_1000025976.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 04-JUL-06
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.2
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SPRING-8
REMARK 200 BEAMLINE : BL26B1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0
REMARK 200 MONOCHROMATOR : GRAPHITE
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 51912
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.600
REMARK 200 RESOLUTION RANGE LOW (A) : 40.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 90.8
REMARK 200 DATA REDUNDANCY : 3.300
REMARK 200 R MERGE (I) : 0.04900
REMARK 200 R SYM (I) : 0.04500
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 19.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.60
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.66
REMARK 200 COMPLETENESS FOR SHELL (%) : 74.7
REMARK 200 DATA REDUNDANCY IN SHELL : 2.60
REMARK 200 R MERGE FOR SHELL (I) : 0.25900
REMARK 200 R SYM FOR SHELL (I) : 0.21800
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.700
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: FOURIER SYNTHESIS
REMARK 200 SOFTWARE USED: CNS 1.1
REMARK 200 STARTING MODEL: 1WQW
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 42.40
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.14
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG20K, ACETATE, NAOH, ATP, BIOTIN, PH
REMARK 280 5.2, MICROBATCH, TEMPERATURE 295K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,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 41.41300
REMARK 290 SMTRY3 2 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 300 REMARK: THE BIOLOGICAL UNIT IS A DIMER AND IDENTICAL TO THE
REMARK 300 ASYMMETRIC UNIT
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: 4790 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 19960 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 1.0 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 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 TRP A 101 NE1 TRP A 101 CE2 0.114
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 ILE A 8 -60.27 -122.49
REMARK 500 VAL A 132 -79.32 -108.52
REMARK 500 ASP A 206 -172.67 177.94
REMARK 500 ASP A 229 48.07 -101.80
REMARK 500 ILE B 8 -58.33 -120.95
REMARK 500 LEU B 49 -140.25 54.10
REMARK 500 ASN B 50 41.27 -106.65
REMARK 500 VAL B 132 -78.54 -112.21
REMARK 500 PRO B 152 108.62 -58.41
REMARK 500 SER B 199 153.92 -49.40
REMARK 500 ASP B 206 -175.08 -177.44
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 ATP A 1301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ATP B 1302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BTN A 1401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BTN B 1402
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1WQW RELATED DB: PDB
REMARK 900 THE APO-PROTEIN COMPLEXED WITH BIOTINYL-5'-AMP
REMARK 900 RELATED ID: 2DXU RELATED DB: PDB
REMARK 900 RELATED ID: PHO001000147.15 RELATED DB: TARGETDB
DBREF 2DXT A 1 235 UNP O57883 O57883_PYRHO 1 235
DBREF 2DXT B 1 235 UNP O57883 O57883_PYRHO 1 235
SEQADV 2DXT ALA A 104 UNP O57883 ASP 104 ENGINEERED MUTATION
SEQADV 2DXT ALA B 104 UNP O57883 ASP 104 ENGINEERED MUTATION
SEQRES 1 A 235 MET LEU GLY LEU LYS THR SER ILE ILE GLY ARG ARG VAL
SEQRES 2 A 235 ILE TYR PHE GLN GLU ILE THR SER THR ASN GLU PHE ALA
SEQRES 3 A 235 LYS THR SER TYR LEU GLU GLU GLY THR VAL ILE VAL ALA
SEQRES 4 A 235 ASP LYS GLN THR MET GLY HIS GLY ARG LEU ASN ARG LYS
SEQRES 5 A 235 TRP GLU SER PRO GLU GLY GLY LEU TRP LEU SER ILE VAL
SEQRES 6 A 235 LEU SER PRO LYS VAL PRO GLN LYS ASP LEU PRO LYS ILE
SEQRES 7 A 235 VAL PHE LEU GLY ALA VAL GLY VAL VAL GLU THR LEU LYS
SEQRES 8 A 235 GLU PHE SER ILE ASP GLY ARG ILE LYS TRP PRO ASN ALA
SEQRES 9 A 235 VAL LEU VAL ASN TYR LYS LYS ILE ALA GLY VAL LEU VAL
SEQRES 10 A 235 GLU GLY LYS GLY ASP LYS ILE VAL LEU GLY ILE GLY LEU
SEQRES 11 A 235 ASN VAL ASN ASN LYS VAL PRO ASN GLY ALA THR SER MET
SEQRES 12 A 235 LYS LEU GLU LEU GLY SER GLU VAL PRO LEU LEU SER VAL
SEQRES 13 A 235 PHE ARG SER LEU ILE THR ASN LEU ASP ARG LEU TYR LEU
SEQRES 14 A 235 ASN PHE LEU LYS ASN PRO MET ASP ILE LEU ASN LEU VAL
SEQRES 15 A 235 ARG ASP ASN MET ILE LEU GLY VAL ARG VAL LYS ILE LEU
SEQRES 16 A 235 GLY ASP GLY SER PHE GLU GLY ILE ALA GLU ASP ILE ASP
SEQRES 17 A 235 ASP PHE GLY ARG LEU ILE ILE ARG LEU ASP SER GLY GLU
SEQRES 18 A 235 VAL LYS LYS VAL ILE TYR GLY ASP VAL SER LEU ARG PHE
SEQRES 19 A 235 LEU
SEQRES 1 B 235 MET LEU GLY LEU LYS THR SER ILE ILE GLY ARG ARG VAL
SEQRES 2 B 235 ILE TYR PHE GLN GLU ILE THR SER THR ASN GLU PHE ALA
SEQRES 3 B 235 LYS THR SER TYR LEU GLU GLU GLY THR VAL ILE VAL ALA
SEQRES 4 B 235 ASP LYS GLN THR MET GLY HIS GLY ARG LEU ASN ARG LYS
SEQRES 5 B 235 TRP GLU SER PRO GLU GLY GLY LEU TRP LEU SER ILE VAL
SEQRES 6 B 235 LEU SER PRO LYS VAL PRO GLN LYS ASP LEU PRO LYS ILE
SEQRES 7 B 235 VAL PHE LEU GLY ALA VAL GLY VAL VAL GLU THR LEU LYS
SEQRES 8 B 235 GLU PHE SER ILE ASP GLY ARG ILE LYS TRP PRO ASN ALA
SEQRES 9 B 235 VAL LEU VAL ASN TYR LYS LYS ILE ALA GLY VAL LEU VAL
SEQRES 10 B 235 GLU GLY LYS GLY ASP LYS ILE VAL LEU GLY ILE GLY LEU
SEQRES 11 B 235 ASN VAL ASN ASN LYS VAL PRO ASN GLY ALA THR SER MET
SEQRES 12 B 235 LYS LEU GLU LEU GLY SER GLU VAL PRO LEU LEU SER VAL
SEQRES 13 B 235 PHE ARG SER LEU ILE THR ASN LEU ASP ARG LEU TYR LEU
SEQRES 14 B 235 ASN PHE LEU LYS ASN PRO MET ASP ILE LEU ASN LEU VAL
SEQRES 15 B 235 ARG ASP ASN MET ILE LEU GLY VAL ARG VAL LYS ILE LEU
SEQRES 16 B 235 GLY ASP GLY SER PHE GLU GLY ILE ALA GLU ASP ILE ASP
SEQRES 17 B 235 ASP PHE GLY ARG LEU ILE ILE ARG LEU ASP SER GLY GLU
SEQRES 18 B 235 VAL LYS LYS VAL ILE TYR GLY ASP VAL SER LEU ARG PHE
SEQRES 19 B 235 LEU
HET ATP A1301 31
HET BTN A1401 16
HET ATP B1302 31
HET BTN B1402 16
HETNAM ATP ADENOSINE-5'-TRIPHOSPHATE
HETNAM BTN BIOTIN
FORMUL 3 ATP 2(C10 H16 N5 O13 P3)
FORMUL 4 BTN 2(C10 H16 N2 O3 S)
FORMUL 7 HOH *564(H2 O)
HELIX 1 1 SER A 21 SER A 29 1 9
HELIX 2 2 GLY A 47 ARG A 51 5 5
HELIX 3 3 PRO A 71 PRO A 76 5 6
HELIX 4 4 LYS A 77 PHE A 93 1 17
HELIX 5 5 SER A 142 GLY A 148 1 7
HELIX 6 6 PRO A 152 ASN A 174 1 23
HELIX 7 7 MET A 176 MET A 186 1 11
HELIX 8 8 SER B 21 SER B 29 1 9
HELIX 9 9 PRO B 71 PRO B 76 5 6
HELIX 10 10 LYS B 77 PHE B 93 1 17
HELIX 11 11 SER B 142 GLY B 148 1 7
HELIX 12 12 PRO B 152 ASN B 174 1 23
HELIX 13 13 MET B 176 MET B 186 1 11
SHEET 1 A14 ARG A 98 LYS A 100 0
SHEET 2 A14 ALA A 104 VAL A 107 -1 O LEU A 106 N ARG A 98
SHEET 3 A14 LYS A 110 LYS A 120 -1 O ILE A 112 N VAL A 105
SHEET 4 A14 LYS A 123 LEU A 130 -1 O VAL A 125 N GLU A 118
SHEET 5 A14 LEU A 60 LEU A 66 -1 N LEU A 66 O ILE A 124
SHEET 6 A14 VAL A 36 ALA A 39 -1 N ILE A 37 O SER A 63
SHEET 7 A14 ARG A 12 PHE A 16 1 N ILE A 14 O VAL A 36
SHEET 8 A14 ARG B 12 ILE B 19 -1 O TYR B 15 N VAL A 13
SHEET 9 A14 VAL B 36 GLN B 42 1 O VAL B 36 N ILE B 14
SHEET 10 A14 LEU B 60 LEU B 66 -1 O SER B 63 N ILE B 37
SHEET 11 A14 LYS B 123 LEU B 130 -1 O ILE B 124 N LEU B 66
SHEET 12 A14 LYS B 110 LYS B 120 -1 N GLU B 118 O VAL B 125
SHEET 13 A14 ALA B 104 VAL B 107 -1 N VAL B 105 O ILE B 112
SHEET 14 A14 ARG B 98 LYS B 100 -1 N ARG B 98 O LEU B 106
SHEET 1 B 5 VAL A 222 VAL A 225 0
SHEET 2 B 5 LEU A 213 ARG A 216 -1 N LEU A 213 O VAL A 225
SHEET 3 B 5 SER A 199 ILE A 207 -1 N ASP A 206 O ILE A 214
SHEET 4 B 5 ARG A 191 LEU A 195 -1 N VAL A 192 O GLY A 202
SHEET 5 B 5 SER A 231 PHE A 234 -1 O SER A 231 N LEU A 195
SHEET 1 C 5 VAL B 222 VAL B 225 0
SHEET 2 C 5 LEU B 213 ARG B 216 -1 N LEU B 213 O VAL B 225
SHEET 3 C 5 PHE B 200 ILE B 207 -1 N ASP B 206 O ILE B 214
SHEET 4 C 5 VAL B 190 ILE B 194 -1 N VAL B 192 O GLY B 202
SHEET 5 C 5 LEU B 232 PHE B 234 -1 O ARG B 233 N LYS B 193
CISPEP 1 TRP A 101 PRO A 102 0 -8.95
CISPEP 2 TRP B 101 PRO B 102 0 0.12
SITE 1 AC1 16 ARG A 48 ARG A 51 LYS A 52 TRP A 53
SITE 2 AC1 16 GLU A 54 LYS A 100 ASN A 103 ALA A 104
SITE 3 AC1 16 LYS A 111 ASN A 131 ALA A 140 TYR A 227
SITE 4 AC1 16 BTN A1401 HOH A1494 HOH A1634 HOH A1670
SITE 1 AC2 15 GLY B 47 ARG B 48 ARG B 51 LYS B 52
SITE 2 AC2 15 TRP B 53 GLU B 54 LYS B 100 ASN B 103
SITE 3 AC2 15 LYS B 111 ASN B 131 ALA B 140 BTN B1402
SITE 4 AC2 15 HOH B1440 HOH B1582 HOH B1655
SITE 1 AC3 15 SER A 21 THR A 22 ASN A 23 GLN A 42
SITE 2 AC3 15 GLY A 45 HIS A 46 GLY A 47 TRP A 53
SITE 3 AC3 15 LEU A 62 ASN A 103 LYS A 111 GLY A 114
SITE 4 AC3 15 ILE A 128 GLY A 129 ATP A1301
SITE 1 AC4 17 SER B 21 THR B 22 ASN B 23 GLN B 42
SITE 2 AC4 17 GLY B 45 HIS B 46 GLY B 47 ARG B 48
SITE 3 AC4 17 TRP B 53 LEU B 62 ASN B 103 LYS B 111
SITE 4 AC4 17 GLY B 114 VAL B 115 ILE B 128 GLY B 129
SITE 5 AC4 17 ATP B1302
CRYST1 38.134 82.826 72.220 90.00 102.53 90.00 P 1 21 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 0.026223 0.000000 0.005828 0.00000
SCALE2 0.000000 0.012074 0.000000 0.00000
SCALE3 0.000000 0.000000 0.014184 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
