HEADER TRANSFERASE 11-APR-06 2DKJ
TITLE CRYSTAL STRUCTURE OF T.TH.HB8 SERINE HYDROXYMETHYLTRANSFERASE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SERINE HYDROXYMETHYLTRANSFERASE;
COMPND 3 CHAIN: A, B;
COMPND 4 EC: 2.1.2.1;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: THERMUS THERMOPHILUS;
SOURCE 3 ORGANISM_TAXID: 300852;
SOURCE 4 STRAIN: HB8;
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: PET11A
KEYWDS PLP DEPENDENT ENZYME, TRANSFERASE, STRUCTURAL GENOMICS, NPPSFA,
KEYWDS 2 NATIONAL PROJECT ON PROTEIN STRUCTURAL AND FUNCTIONAL ANALYSES,
KEYWDS 3 RIKEN STRUCTURAL GENOMICS/PROTEOMICS INITIATIVE, RSGI
EXPDTA X-RAY DIFFRACTION
AUTHOR K.KAI,M.GOTO,I.MIYAHARA,K.HIROTSU,RIKEN STRUCTURAL
AUTHOR 2 GENOMICS/PROTEOMICS INITIATIVE (RSGI)
REVDAT 5 25-OCT-23 2DKJ 1 REMARK LINK
REVDAT 4 13-JUL-11 2DKJ 1 VERSN
REVDAT 3 24-FEB-09 2DKJ 1 VERSN
REVDAT 2 09-OCT-07 2DKJ 1 REMARK AUTHOR KEYWDS
REVDAT 1 24-APR-07 2DKJ 0
JRNL AUTH M.GOTO,K.KAI,I.MIYAHARA,K.HIROTSU
JRNL TITL CRYSTAL STRUCTURE OF T.TH.HB8 SERINE
JRNL TITL 2 HYDROXYMETHYLTRANSFERASE
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.15 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) : 1.15
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 42.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 2.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 1624501.730
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 95.2
REMARK 3 NUMBER OF REFLECTIONS : 299961
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) : 0.180
REMARK 3 FREE R VALUE : 0.190
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 10.000
REMARK 3 FREE R VALUE TEST SET COUNT : 29947
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.001
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) : 1.15
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.22
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 90.50
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 42479
REMARK 3 BIN R VALUE (WORKING SET) : 0.2160
REMARK 3 BIN FREE R VALUE : 0.2270
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 10.00
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 4712
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.003
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 6141
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 40
REMARK 3 SOLVENT ATOMS : 896
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 6.60
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 11.90
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.63000
REMARK 3 B22 (A**2) : -0.04000
REMARK 3 B33 (A**2) : 0.67000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -0.13000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.12
REMARK 3 ESD FROM SIGMAA (A) : 0.08
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) : 0.12
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.08
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.005
REMARK 3 BOND ANGLES (DEGREES) : 1.300
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 22.50
REMARK 3 IMPROPER ANGLES (DEGREES) : 1.050
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) : 0.730 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 1.070 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 14.030; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 6.300 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.40
REMARK 3 BSOL : 61.34
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 : SO4.PAR
REMARK 3 PARAMETER FILE 4 : PARAM.PLP
REMARK 3 PARAMETER FILE 5 : PARAM.ETC
REMARK 3 PARAMETER FILE 6 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : TOP.WAT
REMARK 3 TOPOLOGY FILE 3 : SO4.TOP
REMARK 3 TOPOLOGY FILE 4 : TOP.PLP
REMARK 3 TOPOLOGY FILE 5 : INTSHIFF.TOP
REMARK 3 TOPOLOGY FILE 6 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2DKJ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 13-APR-06.
REMARK 100 THE DEPOSITION ID IS D_1000025523.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 09-JUN-04
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.6
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) : 0.75
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MAR CCD 165 MM
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 302432
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.150
REMARK 200 RESOLUTION RANGE LOW (A) : 53.500
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 95.8
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
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) : 1.15
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.19
REMARK 200 COMPLETENESS FOR SHELL (%) : 90.1
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: AMORE
REMARK 200 STARTING MODEL: PDB ENTRY 1KKJ
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 51.33
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.53
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.8M LITHIUM SULFATE, 0.4M AMMONIUM
REMARK 280 SULFATE, 0.1M SODIUM CITRATE , PH 5.6, VAPOR DIFFUSION, HANGING
REMARK 280 DROP, TEMPERATURE 298K
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 41.44200
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 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,PQS
REMARK 350 TOTAL BURIED SURFACE AREA: 8600 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 25290 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -83.0 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 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 VAL A 2
REMARK 465 SER A 3
REMARK 465 THR A 4
REMARK 465 LEU A 5
REMARK 465 MET B 1
REMARK 465 VAL B 2
REMARK 465 SER B 3
REMARK 465 THR B 4
REMARK 465 LEU B 5
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 LYS A 6 CG CD CE NZ
REMARK 470 ARG A 128 CG CD NE CZ NH1 NH2
REMARK 470 GLU A 153 CG CD OE1 OE2
REMARK 470 GLU A 161 CG CD OE1 OE2
REMARK 470 GLU A 288 CG CD OE1 OE2
REMARK 470 ARG A 352 CG CD NE CZ NH1 NH2
REMARK 470 GLU A 391 CG CD OE1 OE2
REMARK 470 LYS B 6 CG CD CE NZ
REMARK 470 LEU B 117 CG CD1 CD2
REMARK 470 ARG B 128 CG CD NE CZ NH1 NH2
REMARK 470 LYS B 137 CG CD CE NZ
REMARK 470 GLU B 153 CG CD OE1 OE2
REMARK 470 GLU B 154 CG CD OE1 OE2
REMARK 470 LYS B 245 CG CD CE NZ
REMARK 470 LYS B 349 CG CD CE NZ
REMARK 470 ARG B 352 CG CD NE CZ NH1 NH2
REMARK 470 ARG B 399 CG CD NE CZ NH1 NH2
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 ALA A 173 51.85 -143.52
REMARK 500 LYS A 226 -134.98 90.41
REMARK 500 ASN A 311 -144.73 -128.99
REMARK 500 THR A 354 167.58 65.42
REMARK 500 ALA B 58 59.25 -147.11
REMARK 500 ALA B 173 43.56 -147.40
REMARK 500 LYS B 226 -136.63 86.92
REMARK 500 ASN B 311 -146.32 -126.92
REMARK 500 THR B 354 166.00 66.00
REMARK 500 SER B 390 136.61 -172.53
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 SO4 A 2520
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 1520
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PLP A 510
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PLP B 510
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: TTK003000053.1 RELATED DB: TARGETDB
DBREF 2DKJ A 1 407 GB 55772906 BAD71347 1 407
DBREF 2DKJ B 1 407 GB 55772906 BAD71347 1 407
SEQRES 1 A 407 MET VAL SER THR LEU LYS ARG ASP GLU ALA LEU PHE GLU
SEQRES 2 A 407 LEU ILE ALA LEU GLU GLU LYS ARG GLN ARG GLU GLY LEU
SEQRES 3 A 407 GLU LEU ILE ALA SER GLU ASN PHE VAL SER LYS GLN VAL
SEQRES 4 A 407 ARG GLU ALA VAL GLY SER VAL LEU THR ASN LYS TYR ALA
SEQRES 5 A 407 GLU GLY TYR PRO GLY ALA ARG TYR TYR GLY GLY CYS GLU
SEQRES 6 A 407 VAL ILE ASP ARG VAL GLU SER LEU ALA ILE GLU ARG ALA
SEQRES 7 A 407 LYS ALA LEU PHE GLY ALA ALA TRP ALA ASN VAL GLN PRO
SEQRES 8 A 407 HIS SER GLY SER GLN ALA ASN MET ALA VAL TYR MET ALA
SEQRES 9 A 407 LEU MET GLU PRO GLY ASP THR LEU MET GLY MET ASP LEU
SEQRES 10 A 407 ALA ALA GLY GLY HIS LEU THR HIS GLY SER ARG VAL ASN
SEQRES 11 A 407 PHE SER GLY LYS LEU TYR LYS VAL VAL SER TYR GLY VAL
SEQRES 12 A 407 ARG PRO ASP THR GLU LEU ILE ASP LEU GLU GLU VAL ARG
SEQRES 13 A 407 ARG LEU ALA LEU GLU HIS ARG PRO LYS VAL ILE VAL ALA
SEQRES 14 A 407 GLY ALA SER ALA TYR PRO ARG PHE TRP ASP PHE LYS ALA
SEQRES 15 A 407 PHE ARG GLU ILE ALA ASP GLU VAL GLY ALA TYR LEU VAL
SEQRES 16 A 407 VAL ASP MET ALA HIS PHE ALA GLY LEU VAL ALA ALA GLY
SEQRES 17 A 407 LEU HIS PRO ASN PRO LEU PRO TYR ALA HIS VAL VAL THR
SEQRES 18 A 407 SER THR THR HIS LYS THR LEU ARG GLY PRO ARG GLY GLY
SEQRES 19 A 407 LEU ILE LEU SER ASN ASP PRO GLU LEU GLY LYS ARG ILE
SEQRES 20 A 407 ASP LYS LEU ILE PHE PRO GLY ILE GLN GLY GLY PRO LEU
SEQRES 21 A 407 GLU HIS VAL ILE ALA GLY LYS ALA VAL ALA PHE PHE GLU
SEQRES 22 A 407 ALA LEU GLN PRO GLU PHE LYS GLU TYR SER ARG LEU VAL
SEQRES 23 A 407 VAL GLU ASN ALA LYS ARG LEU ALA GLU GLU LEU ALA ARG
SEQRES 24 A 407 ARG GLY TYR ARG ILE VAL THR GLY GLY THR ASP ASN HIS
SEQRES 25 A 407 LEU PHE LEU VAL ASP LEU ARG PRO LYS GLY LEU THR GLY
SEQRES 26 A 407 LYS GLU ALA GLU GLU ARG LEU ASP ALA VAL GLY ILE THR
SEQRES 27 A 407 VAL ASN LYS ASN ALA ILE PRO PHE ASP PRO LYS PRO PRO
SEQRES 28 A 407 ARG VAL THR SER GLY ILE ARG ILE GLY THR PRO ALA ILE
SEQRES 29 A 407 THR THR ARG GLY PHE THR PRO GLU GLU MET PRO LEU VAL
SEQRES 30 A 407 ALA GLU LEU ILE ASP ARG ALA LEU LEU GLU GLY PRO SER
SEQRES 31 A 407 GLU ALA LEU ARG GLU GLU VAL ARG ARG LEU ALA LEU ALA
SEQRES 32 A 407 HIS PRO MET PRO
SEQRES 1 B 407 MET VAL SER THR LEU LYS ARG ASP GLU ALA LEU PHE GLU
SEQRES 2 B 407 LEU ILE ALA LEU GLU GLU LYS ARG GLN ARG GLU GLY LEU
SEQRES 3 B 407 GLU LEU ILE ALA SER GLU ASN PHE VAL SER LYS GLN VAL
SEQRES 4 B 407 ARG GLU ALA VAL GLY SER VAL LEU THR ASN LYS TYR ALA
SEQRES 5 B 407 GLU GLY TYR PRO GLY ALA ARG TYR TYR GLY GLY CYS GLU
SEQRES 6 B 407 VAL ILE ASP ARG VAL GLU SER LEU ALA ILE GLU ARG ALA
SEQRES 7 B 407 LYS ALA LEU PHE GLY ALA ALA TRP ALA ASN VAL GLN PRO
SEQRES 8 B 407 HIS SER GLY SER GLN ALA ASN MET ALA VAL TYR MET ALA
SEQRES 9 B 407 LEU MET GLU PRO GLY ASP THR LEU MET GLY MET ASP LEU
SEQRES 10 B 407 ALA ALA GLY GLY HIS LEU THR HIS GLY SER ARG VAL ASN
SEQRES 11 B 407 PHE SER GLY LYS LEU TYR LYS VAL VAL SER TYR GLY VAL
SEQRES 12 B 407 ARG PRO ASP THR GLU LEU ILE ASP LEU GLU GLU VAL ARG
SEQRES 13 B 407 ARG LEU ALA LEU GLU HIS ARG PRO LYS VAL ILE VAL ALA
SEQRES 14 B 407 GLY ALA SER ALA TYR PRO ARG PHE TRP ASP PHE LYS ALA
SEQRES 15 B 407 PHE ARG GLU ILE ALA ASP GLU VAL GLY ALA TYR LEU VAL
SEQRES 16 B 407 VAL ASP MET ALA HIS PHE ALA GLY LEU VAL ALA ALA GLY
SEQRES 17 B 407 LEU HIS PRO ASN PRO LEU PRO TYR ALA HIS VAL VAL THR
SEQRES 18 B 407 SER THR THR HIS LYS THR LEU ARG GLY PRO ARG GLY GLY
SEQRES 19 B 407 LEU ILE LEU SER ASN ASP PRO GLU LEU GLY LYS ARG ILE
SEQRES 20 B 407 ASP LYS LEU ILE PHE PRO GLY ILE GLN GLY GLY PRO LEU
SEQRES 21 B 407 GLU HIS VAL ILE ALA GLY LYS ALA VAL ALA PHE PHE GLU
SEQRES 22 B 407 ALA LEU GLN PRO GLU PHE LYS GLU TYR SER ARG LEU VAL
SEQRES 23 B 407 VAL GLU ASN ALA LYS ARG LEU ALA GLU GLU LEU ALA ARG
SEQRES 24 B 407 ARG GLY TYR ARG ILE VAL THR GLY GLY THR ASP ASN HIS
SEQRES 25 B 407 LEU PHE LEU VAL ASP LEU ARG PRO LYS GLY LEU THR GLY
SEQRES 26 B 407 LYS GLU ALA GLU GLU ARG LEU ASP ALA VAL GLY ILE THR
SEQRES 27 B 407 VAL ASN LYS ASN ALA ILE PRO PHE ASP PRO LYS PRO PRO
SEQRES 28 B 407 ARG VAL THR SER GLY ILE ARG ILE GLY THR PRO ALA ILE
SEQRES 29 B 407 THR THR ARG GLY PHE THR PRO GLU GLU MET PRO LEU VAL
SEQRES 30 B 407 ALA GLU LEU ILE ASP ARG ALA LEU LEU GLU GLY PRO SER
SEQRES 31 B 407 GLU ALA LEU ARG GLU GLU VAL ARG ARG LEU ALA LEU ALA
SEQRES 32 B 407 HIS PRO MET PRO
HET SO4 A2520 5
HET PLP A 510 15
HET SO4 B1520 5
HET PLP B 510 15
HETNAM SO4 SULFATE ION
HETNAM PLP PYRIDOXAL-5'-PHOSPHATE
HETSYN PLP VITAMIN B6 PHOSPHATE
FORMUL 3 SO4 2(O4 S 2-)
FORMUL 4 PLP 2(C8 H10 N O6 P)
FORMUL 7 HOH *896(H2 O)
HELIX 1 1 ASP A 8 GLU A 24 1 17
HELIX 2 2 SER A 36 GLY A 44 1 9
HELIX 3 3 SER A 45 LYS A 50 5 6
HELIX 4 4 CYS A 64 GLY A 83 1 20
HELIX 5 5 SER A 93 MET A 106 1 14
HELIX 6 6 LEU A 117 GLY A 120 5 4
HELIX 7 7 HIS A 122 GLY A 126 5 5
HELIX 8 8 ASN A 130 TYR A 136 1 7
HELIX 9 9 ASP A 151 ARG A 163 1 13
HELIX 10 10 ASP A 179 GLY A 191 1 13
HELIX 11 11 PHE A 201 ALA A 207 1 7
HELIX 12 12 HIS A 225 ARG A 229 5 5
HELIX 13 13 ASP A 240 PHE A 252 1 13
HELIX 14 14 LEU A 260 GLN A 276 1 17
HELIX 15 15 GLN A 276 ARG A 300 1 25
HELIX 16 16 THR A 306 GLY A 308 5 3
HELIX 17 17 ARG A 319 GLY A 322 5 4
HELIX 18 18 THR A 324 VAL A 335 1 12
HELIX 19 19 THR A 361 ARG A 367 1 7
HELIX 20 20 THR A 370 GLU A 372 5 3
HELIX 21 21 GLU A 373 GLY A 388 1 16
HELIX 22 22 SER A 390 ALA A 403 1 14
HELIX 23 23 ASP B 8 GLY B 25 1 18
HELIX 24 24 SER B 36 GLY B 44 1 9
HELIX 25 25 SER B 45 LYS B 50 5 6
HELIX 26 26 CYS B 64 GLY B 83 1 20
HELIX 27 27 SER B 93 MET B 106 1 14
HELIX 28 28 LEU B 117 GLY B 120 5 4
HELIX 29 29 HIS B 122 GLY B 126 5 5
HELIX 30 30 ASN B 130 TYR B 136 1 7
HELIX 31 31 ASP B 151 ARG B 163 1 13
HELIX 32 32 ASP B 179 VAL B 190 1 12
HELIX 33 33 PHE B 201 ALA B 207 1 7
HELIX 34 34 HIS B 225 ARG B 229 5 5
HELIX 35 35 ASP B 240 PHE B 252 1 13
HELIX 36 36 LEU B 260 LEU B 275 1 16
HELIX 37 37 GLN B 276 ARG B 299 1 24
HELIX 38 38 THR B 306 GLY B 308 5 3
HELIX 39 39 ARG B 319 GLY B 322 5 4
HELIX 40 40 THR B 324 ALA B 334 1 11
HELIX 41 41 THR B 361 ARG B 367 1 7
HELIX 42 42 THR B 370 GLU B 372 5 3
HELIX 43 43 GLU B 373 GLY B 388 1 16
HELIX 44 44 SER B 390 ALA B 403 1 14
SHEET 1 A 2 LEU A 26 GLU A 27 0
SHEET 2 A 2 ILE A 337 THR A 338 1 O THR A 338 N LEU A 26
SHEET 1 B 2 GLY A 54 TYR A 55 0
SHEET 2 B 2 ALA A 58 ARG A 59 -1 O ALA A 58 N TYR A 55
SHEET 1 C 7 TRP A 86 ASN A 88 0
SHEET 2 C 7 GLY A 234 SER A 238 -1 O ILE A 236 N ASN A 88
SHEET 3 C 7 VAL A 219 THR A 223 -1 N VAL A 220 O LEU A 237
SHEET 4 C 7 TYR A 193 ASP A 197 1 N VAL A 196 O THR A 221
SHEET 5 C 7 VAL A 166 ALA A 169 1 N ILE A 167 O TYR A 193
SHEET 6 C 7 THR A 111 MET A 115 1 N MET A 113 O VAL A 168
SHEET 7 C 7 LYS A 137 TYR A 141 1 O LYS A 137 N LEU A 112
SHEET 1 D 4 ARG A 303 ILE A 304 0
SHEET 2 D 4 LEU A 313 ASP A 317 -1 O ASP A 317 N ARG A 303
SHEET 3 D 4 GLY A 356 GLY A 360 -1 O ILE A 357 N VAL A 316
SHEET 4 D 4 ASN A 340 LYS A 341 -1 N ASN A 340 O ARG A 358
SHEET 1 E 2 LEU B 26 GLU B 27 0
SHEET 2 E 2 ILE B 337 THR B 338 1 O THR B 338 N LEU B 26
SHEET 1 F 2 GLY B 54 TYR B 55 0
SHEET 2 F 2 ALA B 58 ARG B 59 -1 O ALA B 58 N TYR B 55
SHEET 1 G 7 TRP B 86 ASN B 88 0
SHEET 2 G 7 GLY B 234 SER B 238 -1 O ILE B 236 N ASN B 88
SHEET 3 G 7 VAL B 219 THR B 223 -1 N VAL B 220 O LEU B 237
SHEET 4 G 7 TYR B 193 ASP B 197 1 N VAL B 196 O THR B 221
SHEET 5 G 7 VAL B 166 ALA B 169 1 N ILE B 167 O VAL B 195
SHEET 6 G 7 THR B 111 MET B 115 1 N MET B 113 O VAL B 168
SHEET 7 G 7 LYS B 137 TYR B 141 1 O LYS B 137 N LEU B 112
SHEET 1 H 4 ARG B 303 ILE B 304 0
SHEET 2 H 4 LEU B 313 ASP B 317 -1 O ASP B 317 N ARG B 303
SHEET 3 H 4 GLY B 356 GLY B 360 -1 O ILE B 357 N VAL B 316
SHEET 4 H 4 ASN B 340 ASN B 342 -1 N ASN B 342 O GLY B 356
LINK NZ LYS A 226 C4A PLP A 510 1555 1555 1.38
LINK NZ LYS B 226 C4A PLP B 510 1555 1555 1.38
CISPEP 1 PHE A 252 PRO A 253 0 0.50
CISPEP 2 PHE B 252 PRO B 253 0 0.49
SITE 1 AC1 8 SER A 31 SER A 172 HIS A 200 LYS A 226
SITE 2 AC1 8 ARG A 358 PLP A 510 TYR B 61 HOH B1846
SITE 1 AC2 11 TYR A 51 TYR A 61 HOH A2589 HOH A2597
SITE 2 AC2 11 SER B 31 SER B 172 HIS B 200 LYS B 226
SITE 3 AC2 11 ARG B 358 PLP B 510 HOH B1708
SITE 1 AC3 17 SER A 93 GLY A 94 SER A 95 HIS A 122
SITE 2 AC3 17 SER A 172 ASP A 197 ALA A 199 HIS A 200
SITE 3 AC3 17 THR A 223 HIS A 225 LYS A 226 SO4 A2520
SITE 4 AC3 17 HOH A2530 HOH A2610 TYR B 51 GLY B 257
SITE 5 AC3 17 GLY B 258
SITE 1 AC4 18 TYR A 51 GLY A 257 GLY A 258 SER B 93
SITE 2 AC4 18 GLY B 94 SER B 95 HIS B 122 THR B 124
SITE 3 AC4 18 HIS B 125 ASP B 197 ALA B 199 HIS B 200
SITE 4 AC4 18 THR B 223 HIS B 225 LYS B 226 SO4 B1520
SITE 5 AC4 18 HOH B1526 HOH B1536
CRYST1 57.988 82.884 94.074 90.00 91.67 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 0.017245 0.000000 0.000504 0.00000
SCALE2 0.000000 0.012065 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010634 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
