HEADER TRANSFERASE 29-NOV-05 2C7T
TITLE CRYSTAL STRUCTURE OF THE PLP-BOUND FORM OF BTRR, A DUAL FUNCTIONAL
TITLE 2 AMINOTRANSFERASE INVOLVED IN BUTIROSIN BIOSYNTHESIS.
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: GLUTAMINE-2-DEOXY-SCYLLO-INOSOSE AMINOTRANSFERASE;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: BTRR - BUTIROSIN BIOSYNTHESIS AMINOTRANSFERASE,;
COMPND 5 EC: 2.6.1.-;
COMPND 6 ENGINEERED: YES;
COMPND 7 OTHER_DETAILS: PLP COFACTOR BOUND
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BACILLUS CIRCULANS;
SOURCE 3 ORGANISM_TAXID: 1397;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 6 EXPRESSION_SYSTEM_PLASMID: PET28A;
SOURCE 7 OTHER_DETAILS: EMBL LOCUS BCI494863, ACCESSION AJ494863.1
KEYWDS AMINOTRANSFERASE, SMAT, BUTIROSIN, AMINOGLYCOSIDE ANTIBIOTICS,
KEYWDS 2 TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR B.POPOVIC,X.TANG,D.Y.CHIRGADZE,F.HUANG,T.L.BLUNDELL,J.B.SPENCER
REVDAT 5 13-DEC-23 2C7T 1 LINK
REVDAT 4 28-MAR-18 2C7T 1 SOURCE JRNL
REVDAT 3 24-FEB-09 2C7T 1 VERSN
REVDAT 2 28-SEP-06 2C7T 1 JRNL
REVDAT 1 16-AUG-06 2C7T 0
JRNL AUTH B.POPOVIC,X.TANG,D.Y.CHIRGADZE,F.HUANG,T.L.BLUNDELL,
JRNL AUTH 2 J.B.SPENCER
JRNL TITL CRYSTAL STRUCTURES OF THE PLP- AND PMP-BOUND FORMS OF BTRR,
JRNL TITL 2 A DUAL FUNCTIONAL AMINOTRANSFERASE INVOLVED IN BUTIROSIN
JRNL TITL 3 BIOSYNTHESIS.
JRNL REF PROTEINS V. 65 220 2006
JRNL REFN ESSN 1097-0134
JRNL PMID 16894611
JRNL DOI 10.1002/PROT.21076
REMARK 2
REMARK 2 RESOLUTION. 2.10 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 : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.10
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 31.33
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 2142803.910
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 99.1
REMARK 3 NUMBER OF REFLECTIONS : 30404
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) : 0.174
REMARK 3 FREE R VALUE : 0.206
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 1536
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.005
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) : 2.10
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.23
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 96.80
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 4604
REMARK 3 BIN R VALUE (WORKING SET) : 0.1900
REMARK 3 BIN FREE R VALUE : 0.2530
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5.40
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 263
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.016
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3185
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 20
REMARK 3 SOLVENT ATOMS : 343
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 17.10
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 25.20
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 3.21000
REMARK 3 B22 (A**2) : 3.21000
REMARK 3 B33 (A**2) : -6.42000
REMARK 3 B12 (A**2) : 1.92000
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) : 0.20
REMARK 3 ESD FROM SIGMAA (A) : 0.12
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) : 0.24
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.19
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.005
REMARK 3 BOND ANGLES (DEGREES) : 1.200
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 22.40
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.780
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) : 1.120 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 1.640 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 1.990 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 2.860 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.34
REMARK 3 BSOL : 47.86
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 : PLP-PATCH.PAR
REMARK 3 PARAMETER FILE 4 : SO4.PAR
REMARK 3 PARAMETER FILE 5 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : WATER_REP.TOP
REMARK 3 TOPOLOGY FILE 3 : PLP.TOP
REMARK 3 TOPOLOGY FILE 4 : SO4.TOP
REMARK 3 TOPOLOGY FILE 5 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: BULK SOLVENT MODEL USED
REMARK 4
REMARK 4 2C7T COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 29-NOV-05.
REMARK 100 THE DEPOSITION ID IS D_1290026575.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 23-FEB-02
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SRS
REMARK 200 BEAMLINE : PX9.5
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.2
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 30455
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.100
REMARK 200 RESOLUTION RANGE LOW (A) : 40.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.2
REMARK 200 DATA REDUNDANCY : 6.500
REMARK 200 R MERGE (I) : 0.07000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 11.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.10
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.15
REMARK 200 COMPLETENESS FOR SHELL (%) : 96.0
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.36000
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: AMORE
REMARK 200 STARTING MODEL: PDB ENTRY 1B9H
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 54.59
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.71
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M AMMONIUM SULPHATE, 15 % PEG 5000
REMARK 280 AND 50 MM MES AT PH 6.5
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32 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+2/3
REMARK 290 3555 -X+Y,-X,Z+1/3
REMARK 290 4555 Y,X,-Z
REMARK 290 5555 X-Y,-Y,-Z+1/3
REMARK 290 6555 -X,-X+Y,-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 108.34667
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 54.17333
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 54.17333
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 108.34667
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: PQS
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 0.00000
REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 127.72143
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 54.17333
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 1
REMARK 465 THR A 2
REMARK 465 ILE A 3
REMARK 465 PRO A 4
REMARK 465 PHE A 5
REMARK 465 HIS A 418
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 ASP A 6 CG OD1 OD2
REMARK 470 HIS A 7 CG ND1 CD2 CE1 NE2
REMARK 470 ARG A 17 CG CD NE CZ NH1 NH2
REMARK 470 GLN A 154 CG CD OE1 NE2
REMARK 470 GLU A 229 CG CD OE1 OE2
REMARK 470 MET A 231 CG SD CE
REMARK 470 LYS A 290 CG CD CE NZ
REMARK 470 LYS A 293 CG CD CE NZ
REMARK 470 GLU A 325 CG CD OE1 OE2
REMARK 470 LYS A 330 CG CD CE NZ
REMARK 470 TYR A 342 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 ARG A 380 CG CD NE CZ NH1 NH2
REMARK 470 GLU A 409 CG CD OE1 OE2
REMARK 470 ARG A 412 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 413 CG CD CE NZ
REMARK 470 THR A 417 CA C O CB OG1 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 PHE A 140 -87.23 56.18
REMARK 500 SER A 167 35.04 -149.49
REMARK 500 ALA A 196 29.37 -141.24
REMARK 500 LYS A 240 -63.06 -141.23
REMARK 500 LYS A 365 -131.26 50.09
REMARK 500 GLN A 384 34.84 -142.30
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH A2019 DISTANCE = 6.45 ANGSTROMS
REMARK 525 HOH A2022 DISTANCE = 5.83 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A1418
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PLP A1417
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2C81 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURES OF THE PLP- AND PMP- BOUND FORMS OF BTRR, A DUAL
REMARK 900 FUNCTIONAL AMINOTRANSFERASE INVOLVED IN BUTIROSIN BIOSYNTHESIS.
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 THE SEQUENCE IS DESCRIBED IN F HUANG ETAL CHEM COMMUN 23,
REMARK 999 2860-2861 (2002)
DBREF 2C7T A 1 418 UNP Q8G8Y2 Q8G8Y2_BACCI 1 418
SEQRES 1 A 418 MET THR ILE PRO PHE ASP HIS TRP PRO GLU TRP PRO GLN
SEQRES 2 A 418 HIS SER ASP ARG THR ARG ARG LYS ILE GLU GLU VAL PHE
SEQRES 3 A 418 GLN SER ASN ARG TRP ALA ILE SER GLY TYR TRP THR GLY
SEQRES 4 A 418 GLU GLU SER MET GLU ARG LYS PHE ALA LYS ALA PHE ALA
SEQRES 5 A 418 ASP PHE ASN GLY VAL PRO TYR CYS VAL PRO THR THR SER
SEQRES 6 A 418 GLY SER THR ALA LEU MET LEU ALA LEU GLU ALA LEU GLY
SEQRES 7 A 418 ILE GLY GLU GLY ASP GLU VAL ILE VAL PRO SER LEU THR
SEQRES 8 A 418 TRP ILE ALA THR ALA THR ALA VAL LEU ASN VAL ASN ALA
SEQRES 9 A 418 LEU PRO VAL PHE VAL ASP VAL GLU ALA ASP THR TYR CYS
SEQRES 10 A 418 ILE ASP PRO GLN LEU ILE LYS SER ALA ILE THR ASP LYS
SEQRES 11 A 418 THR LYS ALA ILE ILE PRO VAL HIS LEU PHE GLY SER MET
SEQRES 12 A 418 ALA ASN MET ASP GLU ILE ASN GLU ILE ALA GLN GLU HIS
SEQRES 13 A 418 ASN LEU PHE VAL ILE GLU ASP CYS ALA GLN SER HIS GLY
SEQRES 14 A 418 SER VAL TRP ASN ASN GLN ARG ALA GLY THR ILE GLY ASP
SEQRES 15 A 418 ILE GLY ALA PHE SER CYS GLN GLN GLY LYS VAL LEU THR
SEQRES 16 A 418 ALA GLY GLU GLY GLY ILE ILE VAL THR LYS ASN PRO ARG
SEQRES 17 A 418 LEU PHE GLU LEU ILE GLN GLN LEU ARG ALA ASP SER ARG
SEQRES 18 A 418 VAL TYR CYS ASP ASP SER SER GLU LEU MET HIS GLY ASP
SEQRES 19 A 418 MET GLN LEU VAL LYS LYS GLY ASP ILE GLN GLY SER ASN
SEQRES 20 A 418 TYR CYS LEU SER GLU PHE GLN SER ALA ILE LEU LEU ASP
SEQRES 21 A 418 GLN LEU GLN GLU LEU ASP ASP LYS ASN ALA ILE ARG GLU
SEQRES 22 A 418 LYS ASN ALA MET PHE LEU ASN ASP ALA LEU SER LYS ILE
SEQRES 23 A 418 ASP GLY ILE LYS VAL MET LYS ARG PRO PRO GLN VAL SER
SEQRES 24 A 418 ARG GLN THR TYR TYR GLY TYR VAL PHE ARG PHE ASP PRO
SEQRES 25 A 418 VAL LYS PHE GLY GLY LEU ASN ALA ASP GLN PHE CYS GLU
SEQRES 26 A 418 ILE LEU ARG GLU LYS LEU ASN MET GLY THR PHE TYR LEU
SEQRES 27 A 418 HIS PRO PRO TYR LEU PRO VAL HIS LYS ASN PRO LEU PHE
SEQRES 28 A 418 CYS PRO TRP THR LYS ASN ARG TYR LEU LYS SER VAL ARG
SEQRES 29 A 418 LYS THR GLU ALA TYR TRP ARG GLY LEU HIS TYR PRO VAL
SEQRES 30 A 418 SER GLU ARG ALA SER GLY GLN SER ILE VAL ILE HIS HIS
SEQRES 31 A 418 ALA ILE LEU LEU ALA GLU PRO SER HIS LEU SER LEU LEU
SEQRES 32 A 418 VAL ASP ALA VAL ALA GLU LEU ALA ARG LYS PHE CYS VAL
SEQRES 33 A 418 THR HIS
HET PLP A1417 15
HET SO4 A1418 5
HETNAM PLP PYRIDOXAL-5'-PHOSPHATE
HETNAM SO4 SULFATE ION
HETSYN PLP VITAMIN B6 PHOSPHATE
FORMUL 2 PLP C8 H10 N O6 P
FORMUL 3 SO4 O4 S 2-
FORMUL 4 HOH *343(H2 O)
HELIX 1 1 SER A 15 ASN A 29 1 15
HELIX 2 2 SER A 42 GLY A 56 1 15
HELIX 3 3 SER A 65 LEU A 77 1 13
HELIX 4 4 ILE A 93 VAL A 102 1 10
HELIX 5 5 ASP A 119 ILE A 127 1 9
HELIX 6 6 ASN A 145 ASN A 157 1 13
HELIX 7 7 ASN A 206 ALA A 218 1 13
HELIX 8 8 SER A 251 GLN A 263 1 13
HELIX 9 9 GLU A 264 SER A 284 1 21
HELIX 10 10 PRO A 312 PHE A 315 5 4
HELIX 11 11 ASN A 319 ASN A 332 1 14
HELIX 12 12 PRO A 344 ASN A 348 5 5
HELIX 13 13 CYS A 352 LYS A 356 5 5
HELIX 14 14 LEU A 360 LYS A 365 1 6
HELIX 15 15 THR A 366 GLY A 372 1 7
HELIX 16 16 TYR A 375 SER A 382 1 8
HELIX 17 17 ALA A 391 ALA A 395 5 5
HELIX 18 18 GLU A 396 CYS A 415 1 20
SHEET 1 AA 7 TYR A 59 THR A 63 0
SHEET 2 AA 7 GLY A 200 THR A 204 -1 O GLY A 200 N THR A 63
SHEET 3 AA 7 ILE A 183 SER A 187 -1 O GLY A 184 N VAL A 203
SHEET 4 AA 7 PHE A 159 ASP A 163 1 O GLU A 162 N ALA A 185
SHEET 5 AA 7 THR A 131 ILE A 134 1 O LYS A 132 N PHE A 159
SHEET 6 AA 7 GLU A 84 PRO A 88 1 O GLU A 84 N LYS A 132
SHEET 7 AA 7 LEU A 105 VAL A 109 1 O LEU A 105 N VAL A 85
SHEET 1 AB 3 GLN A 175 ARG A 176 0
SHEET 2 AB 3 VAL A 171 TRP A 172 -1 O TRP A 172 N GLN A 175
SHEET 3 AB 3 VAL A 298 ARG A 300 -1 N SER A 299 O VAL A 171
SHEET 1 AC 2 ARG A 221 TYR A 223 0
SHEET 2 AC 2 LEU A 237 LYS A 239 -1 O VAL A 238 N VAL A 222
SHEET 1 AD 4 ILE A 289 VAL A 291 0
SHEET 2 AD 4 GLY A 305 PHE A 310 -1 O ARG A 309 N LYS A 290
SHEET 3 AD 4 SER A 385 HIS A 389 -1 O ILE A 386 N PHE A 308
SHEET 4 AD 4 LEU A 338 HIS A 339 -1 O HIS A 339 N VAL A 387
LINK NZ LYS A 192 C4A PLP A1417 1555 1555 1.38
CISPEP 1 TRP A 11 PRO A 12 0 0.10
SITE 1 AC1 5 TRP A 92 PHE A 140 TYR A 304 HIS A 339
SITE 2 AC1 5 HOH A2343
SITE 1 AC2 15 SER A 65 GLY A 66 SER A 67 THR A 91
SITE 2 AC2 15 TRP A 92 VAL A 137 ASP A 163 ALA A 165
SITE 3 AC2 15 GLN A 166 SER A 187 LYS A 192 ASN A 247
SITE 4 AC2 15 HOH A2340 HOH A2341 HOH A2342
CRYST1 73.740 73.740 162.520 90.00 90.00 120.00 P 32 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 0.013561 0.007830 0.000000 0.00000
SCALE2 0.000000 0.015659 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006153 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
