HEADER LYASE 15-JUL-06 2DTT
TITLE CRYSTAL STRUCTURE OF 6-PYRUVOYL TETRAHYDROBIOPTERIN SYNTHASE FROM
TITLE 2 PYROCOCCUS HORIKOSHII OT3 COMPLEXED WITH (1'R,2'S)-BIOPTERIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HYPOTHETICAL PROTEIN PH0634;
COMPND 3 CHAIN: A, B, C, D, E, F;
COMPND 4 SYNONYM: 6-PYRUVOYL TETRAHYDROBIOPTERIN SYNTHASE;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: PYROCOCCUS HORIKOSHII;
SOURCE 3 ORGANISM_TAXID: 70601;
SOURCE 4 STRAIN: OT3;
SOURCE 5 GENE: PH0634;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: (DE3)RIL;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET 11A
KEYWDS 6-PYRUVOYL TETRAHYDROBIOPTERIN SYNTHASE (PTPS), BIOPTERIN, STRUCTURAL
KEYWDS 2 GENOMICS, NPPSFA, NATIONAL PROJECT ON PROTEIN STRUCTURAL AND
KEYWDS 3 FUNCTIONAL ANALYSES, RIKEN STRUCTURAL GENOMICS/PROTEOMICS
KEYWDS 4 INITIATIVE, RSGI, LYASE
EXPDTA X-RAY DIFFRACTION
AUTHOR B.BAGAUTDINOV,N.KUNISHIMA,RIKEN STRUCTURAL GENOMICS/PROTEOMICS
AUTHOR 2 INITIATIVE (RSGI)
REVDAT 4 25-OCT-23 2DTT 1 REMARK
REVDAT 3 13-JUL-11 2DTT 1 VERSN
REVDAT 2 24-FEB-09 2DTT 1 VERSN
REVDAT 1 15-JAN-07 2DTT 0
JRNL AUTH B.BAGAUTDINOV,N.KUNISHIMA
JRNL TITL CRYSTAL STRUCTURE OF 6-PYRUVOYL TETRAHYDROBIOPTERIN SYNTHASE
JRNL TITL 2 FROM PYROCOCCUS HORIKOSHII OT3
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.20 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) : 2.20
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 35.68
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) (%) : 90.4
REMARK 3 NUMBER OF REFLECTIONS : 32611
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) : 0.195
REMARK 3 FREE R VALUE : 0.236
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : 1637
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) : 2.20
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.28
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 79.40
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.2310
REMARK 3 BIN FREE R VALUE : 0.2720
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 131
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.024
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 5403
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 102
REMARK 3 SOLVENT ATOMS : 405
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 32.70
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 38.80
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 3.25000
REMARK 3 B22 (A**2) : 2.24000
REMARK 3 B33 (A**2) : -5.48000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -6.17000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.24
REMARK 3 ESD FROM SIGMAA (A) : 0.21
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) : 0.31
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.26
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) : 24.30
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.650
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 2DTT COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 19-JUL-06.
REMARK 100 THE DEPOSITION ID IS D_1000025834.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 21-MAY-06
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.25
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
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 : 32611
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.200
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 (%) : 90.4
REMARK 200 DATA REDUNDANCY : 3.000
REMARK 200 R MERGE (I) : 0.07200
REMARK 200 R SYM (I) : 0.06700
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 8.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.20
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.28
REMARK 200 COMPLETENESS FOR SHELL (%) : 81.4
REMARK 200 DATA REDUNDANCY IN SHELL : 3.00
REMARK 200 R MERGE FOR SHELL (I) : 0.22900
REMARK 200 R SYM FOR SHELL (I) : 0.22500
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.100
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: 2DJ6
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 44.77
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.23
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 16.5% PEG 20000, 0.1M ACETATE, NAOH
REMARK 280 PH6.25, 3MM BIOPTERIN, MICROBATHCH, TEMPERATURE 291K
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 52.72250
REMARK 290 SMTRY3 2 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 300 REMARK: BIOLOGICAL ASSEMBLY IS A TRIMER. IN THE ASSYMMETRIC UNIT
REMARK 300 SUBUNITS (A,B,C) AND (D,E,F) REPRESENT BIOLOGICAL UNITS
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: 5960 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 15300 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -6.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C
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: 6040 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 15310 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -3.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D, 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 VAL A 17
REMARK 465 LYS A 18
REMARK 465 VAL A 19
REMARK 465 GLY A 20
REMARK 465 ASP A 21
REMARK 465 HIS A 22
REMARK 465 TRP A 23
REMARK 465 GLU A 24
REMARK 465 ASP A 25
REMARK 465 VAL A 26
REMARK 465 ALA C 16
REMARK 465 VAL C 17
REMARK 465 LYS C 18
REMARK 465 VAL C 19
REMARK 465 GLY C 20
REMARK 465 ASP C 21
REMARK 465 HIS C 22
REMARK 465 TRP C 23
REMARK 465 GLU C 24
REMARK 465 ASP C 25
REMARK 465 ALA D 16
REMARK 465 VAL D 17
REMARK 465 LYS D 18
REMARK 465 VAL D 19
REMARK 465 GLY D 20
REMARK 465 ASP D 21
REMARK 465 HIS D 22
REMARK 465 TRP D 23
REMARK 465 GLU D 24
REMARK 465 ASP D 25
REMARK 465 VAL D 26
REMARK 465 ALA F 16
REMARK 465 VAL F 17
REMARK 465 LYS F 18
REMARK 465 VAL F 19
REMARK 465 GLY F 20
REMARK 465 ASP F 21
REMARK 465 HIS F 22
REMARK 465 TRP F 23
REMARK 465 GLU F 24
REMARK 465 ASP F 25
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 B 23 NE1 TRP B 23 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 HIS A 65 52.24 36.58
REMARK 500 PRO A 75 53.86 -68.98
REMARK 500 VAL B 19 61.35 -115.62
REMARK 500 PRO B 75 46.75 -69.70
REMARK 500 PRO B 94 1.53 -67.71
REMARK 500 MET C 47 134.98 179.04
REMARK 500 TYR C 95 51.82 -104.20
REMARK 500 MET D 47 148.90 -171.98
REMARK 500 HIS D 65 51.38 39.68
REMARK 500 ASN D 67 90.52 -63.15
REMARK 500 LEU D 68 -16.35 -46.26
REMARK 500 ASN D 70 -43.37 -143.98
REMARK 500 PRO D 75 49.44 -66.65
REMARK 500 LYS D 107 -19.91 -158.36
REMARK 500 ALA E 13 149.33 -176.19
REMARK 500 VAL E 19 66.54 -108.77
REMARK 500 HIS E 22 -160.34 -116.54
REMARK 500 MET F 47 142.50 179.48
REMARK 500 PRO F 75 50.15 -67.16
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 H4B B 1001
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE H4B C 1002
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE H4B A 1003
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE H4B E 1004
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE H4B F 1005
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE H4B D 1006
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2DJ6 RELATED DB: PDB
REMARK 900 THE SAME PROTEIN
REMARK 900 RELATED ID: PHO001000634.2 RELATED DB: TARGETDB
DBREF 2DTT A 1 115 UNP O58368 O58368_PYRHO 1 115
DBREF 2DTT B 1 115 UNP O58368 O58368_PYRHO 1 115
DBREF 2DTT C 1 115 UNP O58368 O58368_PYRHO 1 115
DBREF 2DTT D 1 115 UNP O58368 O58368_PYRHO 1 115
DBREF 2DTT E 1 115 UNP O58368 O58368_PYRHO 1 115
DBREF 2DTT F 1 115 UNP O58368 O58368_PYRHO 1 115
SEQRES 1 A 115 MET LYS SER ARG ILE ILE VAL ARG THR SER PHE ASP ALA
SEQRES 2 A 115 ALA HIS ALA VAL LYS VAL GLY ASP HIS TRP GLU ASP VAL
SEQRES 3 A 115 HIS GLY HIS THR PHE PHE LEU GLU VAL ALA ILE GLU GLY
SEQRES 4 A 115 GLU ILE LYS ASN GLY TYR VAL MET ASP PHE LEU GLU LEU
SEQRES 5 A 115 ARG LYS ILE VAL GLU GLU ILE THR LYS GLU LEU ASP HIS
SEQRES 6 A 115 ARG ASN LEU ASN ASN ILE PHE GLU ASN PRO THR THR GLU
SEQRES 7 A 115 ASN ILE ALA LEU TRP ILE GLY GLU ARG ILE ARG ASP LYS
SEQRES 8 A 115 LEU PRO PRO TYR VAL LYS LEU LYS ARG VAL VAL LEU TRP
SEQRES 9 A 115 GLU GLY LYS ASP ASN GLY VAL GLU LEU GLU TRP
SEQRES 1 B 115 MET LYS SER ARG ILE ILE VAL ARG THR SER PHE ASP ALA
SEQRES 2 B 115 ALA HIS ALA VAL LYS VAL GLY ASP HIS TRP GLU ASP VAL
SEQRES 3 B 115 HIS GLY HIS THR PHE PHE LEU GLU VAL ALA ILE GLU GLY
SEQRES 4 B 115 GLU ILE LYS ASN GLY TYR VAL MET ASP PHE LEU GLU LEU
SEQRES 5 B 115 ARG LYS ILE VAL GLU GLU ILE THR LYS GLU LEU ASP HIS
SEQRES 6 B 115 ARG ASN LEU ASN ASN ILE PHE GLU ASN PRO THR THR GLU
SEQRES 7 B 115 ASN ILE ALA LEU TRP ILE GLY GLU ARG ILE ARG ASP LYS
SEQRES 8 B 115 LEU PRO PRO TYR VAL LYS LEU LYS ARG VAL VAL LEU TRP
SEQRES 9 B 115 GLU GLY LYS ASP ASN GLY VAL GLU LEU GLU TRP
SEQRES 1 C 115 MET LYS SER ARG ILE ILE VAL ARG THR SER PHE ASP ALA
SEQRES 2 C 115 ALA HIS ALA VAL LYS VAL GLY ASP HIS TRP GLU ASP VAL
SEQRES 3 C 115 HIS GLY HIS THR PHE PHE LEU GLU VAL ALA ILE GLU GLY
SEQRES 4 C 115 GLU ILE LYS ASN GLY TYR VAL MET ASP PHE LEU GLU LEU
SEQRES 5 C 115 ARG LYS ILE VAL GLU GLU ILE THR LYS GLU LEU ASP HIS
SEQRES 6 C 115 ARG ASN LEU ASN ASN ILE PHE GLU ASN PRO THR THR GLU
SEQRES 7 C 115 ASN ILE ALA LEU TRP ILE GLY GLU ARG ILE ARG ASP LYS
SEQRES 8 C 115 LEU PRO PRO TYR VAL LYS LEU LYS ARG VAL VAL LEU TRP
SEQRES 9 C 115 GLU GLY LYS ASP ASN GLY VAL GLU LEU GLU TRP
SEQRES 1 D 115 MET LYS SER ARG ILE ILE VAL ARG THR SER PHE ASP ALA
SEQRES 2 D 115 ALA HIS ALA VAL LYS VAL GLY ASP HIS TRP GLU ASP VAL
SEQRES 3 D 115 HIS GLY HIS THR PHE PHE LEU GLU VAL ALA ILE GLU GLY
SEQRES 4 D 115 GLU ILE LYS ASN GLY TYR VAL MET ASP PHE LEU GLU LEU
SEQRES 5 D 115 ARG LYS ILE VAL GLU GLU ILE THR LYS GLU LEU ASP HIS
SEQRES 6 D 115 ARG ASN LEU ASN ASN ILE PHE GLU ASN PRO THR THR GLU
SEQRES 7 D 115 ASN ILE ALA LEU TRP ILE GLY GLU ARG ILE ARG ASP LYS
SEQRES 8 D 115 LEU PRO PRO TYR VAL LYS LEU LYS ARG VAL VAL LEU TRP
SEQRES 9 D 115 GLU GLY LYS ASP ASN GLY VAL GLU LEU GLU TRP
SEQRES 1 E 115 MET LYS SER ARG ILE ILE VAL ARG THR SER PHE ASP ALA
SEQRES 2 E 115 ALA HIS ALA VAL LYS VAL GLY ASP HIS TRP GLU ASP VAL
SEQRES 3 E 115 HIS GLY HIS THR PHE PHE LEU GLU VAL ALA ILE GLU GLY
SEQRES 4 E 115 GLU ILE LYS ASN GLY TYR VAL MET ASP PHE LEU GLU LEU
SEQRES 5 E 115 ARG LYS ILE VAL GLU GLU ILE THR LYS GLU LEU ASP HIS
SEQRES 6 E 115 ARG ASN LEU ASN ASN ILE PHE GLU ASN PRO THR THR GLU
SEQRES 7 E 115 ASN ILE ALA LEU TRP ILE GLY GLU ARG ILE ARG ASP LYS
SEQRES 8 E 115 LEU PRO PRO TYR VAL LYS LEU LYS ARG VAL VAL LEU TRP
SEQRES 9 E 115 GLU GLY LYS ASP ASN GLY VAL GLU LEU GLU TRP
SEQRES 1 F 115 MET LYS SER ARG ILE ILE VAL ARG THR SER PHE ASP ALA
SEQRES 2 F 115 ALA HIS ALA VAL LYS VAL GLY ASP HIS TRP GLU ASP VAL
SEQRES 3 F 115 HIS GLY HIS THR PHE PHE LEU GLU VAL ALA ILE GLU GLY
SEQRES 4 F 115 GLU ILE LYS ASN GLY TYR VAL MET ASP PHE LEU GLU LEU
SEQRES 5 F 115 ARG LYS ILE VAL GLU GLU ILE THR LYS GLU LEU ASP HIS
SEQRES 6 F 115 ARG ASN LEU ASN ASN ILE PHE GLU ASN PRO THR THR GLU
SEQRES 7 F 115 ASN ILE ALA LEU TRP ILE GLY GLU ARG ILE ARG ASP LYS
SEQRES 8 F 115 LEU PRO PRO TYR VAL LYS LEU LYS ARG VAL VAL LEU TRP
SEQRES 9 F 115 GLU GLY LYS ASP ASN GLY VAL GLU LEU GLU TRP
HET H4B A1003 17
HET H4B B1001 17
HET H4B C1002 17
HET H4B D1006 17
HET H4B E1004 17
HET H4B F1005 17
HETNAM H4B 5,6,7,8-TETRAHYDROBIOPTERIN
FORMUL 7 H4B 6(C9 H15 N5 O3)
FORMUL 13 HOH *405(H2 O)
HELIX 1 1 ASP A 48 LYS A 61 1 14
HELIX 2 2 ASN A 67 ILE A 71 5 5
HELIX 3 3 THR A 76 ASP A 90 1 15
HELIX 4 4 ASP B 48 GLU B 62 1 15
HELIX 5 5 ASN B 69 ILE B 71 5 3
HELIX 6 6 THR B 76 LEU B 92 1 17
HELIX 7 7 ASP C 48 LYS C 61 1 14
HELIX 8 8 ASN C 67 ILE C 71 5 5
HELIX 9 9 THR C 76 LEU C 92 1 17
HELIX 10 10 ASP D 48 GLU D 62 1 15
HELIX 11 11 THR D 76 ASP D 90 1 15
HELIX 12 12 ASP E 48 LYS E 61 1 14
HELIX 13 13 ASN E 69 ILE E 71 5 3
HELIX 14 14 THR E 76 LEU E 92 1 17
HELIX 15 15 ASP F 48 LYS F 61 1 14
HELIX 16 16 ASN F 69 ILE F 71 5 3
HELIX 17 17 THR F 76 ASP F 90 1 15
SHEET 1 A14 ARG B 66 ASN B 67 0
SHEET 2 A14 LYS B 2 HIS B 15 1 N ALA B 14 O ARG B 66
SHEET 3 A14 ASN C 109 GLU C 114 -1 O GLY C 110 N ILE B 6
SHEET 4 A14 LYS C 97 GLU C 105 -1 N VAL C 101 O LEU C 113
SHEET 5 A14 HIS C 29 GLY C 39 -1 N GLU C 34 O VAL C 102
SHEET 6 A14 LYS C 2 ALA C 13 -1 N ALA C 13 O HIS C 29
SHEET 7 A14 ASN A 109 GLU A 114 -1 N GLY A 110 O ILE C 6
SHEET 8 A14 VAL A 96 GLU A 105 -1 N VAL A 101 O LEU A 113
SHEET 9 A14 GLY A 28 GLY A 39 -1 N PHE A 32 O TRP A 104
SHEET 10 A14 LYS A 2 ALA A 14 -1 N PHE A 11 O PHE A 31
SHEET 11 A14 ASN B 109 GLU B 114 -1 O GLY B 110 N ILE A 6
SHEET 12 A14 LYS B 97 GLU B 105 -1 N GLU B 105 O ASN B 109
SHEET 13 A14 HIS B 27 GLU B 38 -1 N PHE B 32 O TRP B 104
SHEET 14 A14 LYS B 2 HIS B 15 -1 N PHE B 11 O PHE B 31
SHEET 1 B11 ARG E 66 ASN E 67 0
SHEET 2 B11 LYS E 2 HIS E 15 1 N ALA E 14 O ARG E 66
SHEET 3 B11 HIS E 27 GLU E 38 -1 O PHE E 31 N PHE E 11
SHEET 4 B11 LYS E 97 GLU E 105 -1 O TRP E 104 N PHE E 32
SHEET 5 B11 ASN E 109 GLU E 114 -1 O LEU E 113 N VAL E 101
SHEET 6 B11 LYS D 2 ALA D 13 -1 N ILE D 6 O GLY E 110
SHEET 7 B11 HIS D 29 GLY D 39 -1 O PHE D 31 N PHE D 11
SHEET 8 B11 VAL D 96 GLU D 105 -1 O TRP D 104 N PHE D 32
SHEET 9 B11 ASN D 109 GLU D 114 -1 O LEU D 113 N VAL D 101
SHEET 10 B11 LYS F 2 ALA F 14 -1 O ILE F 6 N GLY D 110
SHEET 11 B11 ARG F 66 ASN F 67 1 O ARG F 66 N ALA F 14
SHEET 1 C 7 ARG E 66 ASN E 67 0
SHEET 2 C 7 LYS E 2 HIS E 15 1 N ALA E 14 O ARG E 66
SHEET 3 C 7 ASN F 109 GLU F 114 -1 O GLY F 110 N ILE E 6
SHEET 4 C 7 VAL F 96 GLU F 105 -1 N VAL F 101 O LEU F 113
SHEET 5 C 7 GLY F 28 GLY F 39 -1 N PHE F 32 O TRP F 104
SHEET 6 C 7 LYS F 2 ALA F 14 -1 N THR F 9 O LEU F 33
SHEET 7 C 7 ARG F 66 ASN F 67 1 O ARG F 66 N ALA F 14
SITE 1 AC1 10 TYR A 45 MET A 47 ASP A 48 PHE A 49
SITE 2 AC1 10 GLU B 24 HIS B 27 THR B 76 THR B 77
SITE 3 AC1 10 GLU B 78 GLU B 105
SITE 1 AC2 7 TYR B 45 MET B 47 ASP B 48 PHE B 49
SITE 2 AC2 7 THR C 77 GLU C 78 GLU C 105
SITE 1 AC3 11 HIS A 15 HIS A 27 HIS A 29 THR A 76
SITE 2 AC3 11 THR A 77 GLU A 78 GLU A 105 TYR C 45
SITE 3 AC3 11 MET C 47 ASP C 48 PHE C 49
SITE 1 AC4 8 PHE D 49 HOH D1025 HIS E 15 THR E 76
SITE 2 AC4 8 THR E 77 GLU E 78 GLU E 105 HOH E1071
SITE 1 AC5 10 TYR E 45 MET E 47 ASP E 48 PHE E 49
SITE 2 AC5 10 HOH E1025 HIS F 29 THR F 76 THR F 77
SITE 3 AC5 10 GLU F 78 GLU F 105
SITE 1 AC6 11 HIS D 15 HIS D 27 HIS D 29 THR D 76
SITE 2 AC6 11 THR D 77 GLU D 78 GLU D 105 TYR F 45
SITE 3 AC6 11 MET F 47 ASP F 48 PHE F 49
CRYST1 35.682 105.445 96.147 90.00 90.95 90.00 P 1 21 1 12
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 0.028025 0.000000 0.000465 0.00000
SCALE2 0.000000 0.009484 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010402 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
