HEADER TRANSFERASE 28-NOV-07 2VIB
TITLE CRYSTAL STRUCTURE OF S172ABSSHMT OBTAINED IN THE PRESENCE OF L-ALLO-
TITLE 2 THR
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SERINE HYDROXYMETHYLTRANSFERASE;
COMPND 3 CHAIN: A;
COMPND 4 EC: 2.1.2.1;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: GEOBACILLUS STEAROTHERMOPHILUS;
SOURCE 3 ORGANISM_TAXID: 1422;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 6 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE 7 EXPRESSION_SYSTEM_VECTOR: PRSETC
KEYWDS ONE-CARBON METABOLISM, SERINE HYDROXYMETHYLTRANSFERASE, TRANSFERASE,
KEYWDS 2 PLP-DEPENDENT, PYRIDOXAL PHOSPHATE
EXPDTA X-RAY DIFFRACTION
AUTHOR V.RAJARAM,B.S.BHAVANI,V.PRAKASH,N.APPAJI RAO,H.S.SAVITHRI,
AUTHOR 2 M.R.N.MURTHY
REVDAT 3 13-DEC-23 2VIB 1 LINK
REVDAT 2 24-FEB-09 2VIB 1 VERSN
REVDAT 1 18-DEC-07 2VIB 0
JRNL AUTH V.RAJARAM,B.S.BHAVANI,V.PRAKASH,N.APPAJI RAO,H.S.SAVITHRI,
JRNL AUTH 2 M.R.N.MURTHY
JRNL TITL CRYSTAL STRUCTURE OF S172ABSSHMT AND ITS COMPLEXES
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.85 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0019
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.85
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 22.43
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 95.7
REMARK 3 NUMBER OF REFLECTIONS : 29678
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 + TEST SET) : 0.173
REMARK 3 R VALUE (WORKING SET) : 0.171
REMARK 3 FREE R VALUE : 0.211
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 1586
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.85
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.90
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2171
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.2950
REMARK 3 BIN FREE R VALUE SET COUNT : 124
REMARK 3 BIN FREE R VALUE : 0.3600
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3115
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 41
REMARK 3 SOLVENT ATOMS : 415
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 20.50
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 18.08
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.00000
REMARK 3 B22 (A**2) : 0.00000
REMARK 3 B33 (A**2) : 0.00000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.158
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.141
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.091
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.999
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.960
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.938
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 3254 ; 0.009 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 4425 ; 1.131 ; 1.967
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 417 ; 5.390 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 150 ;36.862 ;24.133
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 533 ;13.327 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 21 ;14.243 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 493 ; 0.078 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2486 ; 0.004 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 1697 ; 0.192 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 2246 ; 0.298 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 339 ; 0.106 ; 0.200
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 100 ; 0.160 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 68 ; 0.145 ; 0.200
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 2102 ; 0.500 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 3266 ; 0.691 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1294 ; 1.275 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1152 ; 2.024 ; 4.500
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.40
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS.
REMARK 4
REMARK 4 2VIB COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 28-NOV-07.
REMARK 100 THE DEPOSITION ID IS D_1290034566.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU RU200
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : NI FILTER
REMARK 200 OPTICS : OSMIC MIRROR
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
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 : 31269
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.850
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 95.7
REMARK 200 DATA REDUNDANCY : 3.100
REMARK 200 R MERGE (I) : 0.08000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 12.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.85
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.92
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.4
REMARK 200 DATA REDUNDANCY IN SHELL : 2.90
REMARK 200 R MERGE FOR SHELL (I) : 0.41000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.300
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: FOURIER SYNTHESIS
REMARK 200 SOFTWARE USED: REFMAC
REMARK 200 STARTING MODEL: PDB ENTRY 1KL1
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 41.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.10
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 50% MPD 0.1 M HEPES 7.5 0.2 MM EDTA 5
REMARK 280 MM 2-MERCAPTOETHANOL 10 MM L-ALLO-THR, PH 7.5
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z
REMARK 290 3555 -X+1/2,Y+1/2,-Z
REMARK 290 4555 X+1/2,-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 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 30.62000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 53.16500
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 30.62000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 53.16500
REMARK 290 SMTRY3 4 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: PQS
REMARK 350 TOTAL BURIED SURFACE AREA: 8740 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 32700 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -52.5 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 0.00000
REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 0.00000
REMARK 400
REMARK 400 COMPOUND
REMARK 400 ENGINEERED RESIDUE IN CHAIN A, SER 172 TO ALA
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 52 44.48 -144.68
REMARK 500 HIS A 125 40.34 -108.28
REMARK 500 HIS A 148 16.11 58.53
REMARK 500 ALA A 170 169.80 109.25
REMARK 500 ALA A 173 53.36 -148.93
REMARK 500 LYS A 226 -114.92 -94.49
REMARK 500 LYS A 226 -114.28 -94.88
REMARK 500 SER A 305 -0.02 73.03
REMARK 500 ASN A 310 -143.87 -130.29
REMARK 500 THR A 353 162.76 71.00
REMARK 500 ASN A 386 47.33 -142.67
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 A2017 DISTANCE = 6.10 ANGSTROMS
REMARK 525 HOH A2028 DISTANCE = 5.86 ANGSTROMS
REMARK 525 HOH A2036 DISTANCE = 6.82 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PLP A1406
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GLY A1407
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MPD A1408
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MPD A1409
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A1410
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1KL2 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF SERINE HYDROXYMETHYLTRANSFERASECOMPLEXED WITH
REMARK 900 GLYCINE AND 5-FORMYL TETRAHYDROFOLATE
REMARK 900 RELATED ID: 1YJS RELATED DB: PDB
REMARK 900 K226Q MUTANT OF SERINE HYDROXYMETHYLTRANSFERASE FROM
REMARK 900 B.STEAROTHERMOPHILUS, COMPLEX WITH GLYCINE
REMARK 900 RELATED ID: 2VGT RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF E53QBSSHMT WITH GLYCINE
REMARK 900 RELATED ID: 2VGV RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF E53QBSSHMT OBTAINED IN THE PRESENCE OF L-ALLO-
REMARK 900 THREONINE
REMARK 900 RELATED ID: 2VGW RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF E53QBSSHMT OBTAINED IN THE PRESENCE OF GLYCINE
REMARK 900 AND 5-FOMYL TETRAHYDROFOLATE
REMARK 900 RELATED ID: 1KKJ RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF SERINE HYDROXYMETHYLTRANSFERASE
REMARK 900 FROMB.STEAROTHERMOPHILUS
REMARK 900 RELATED ID: 1KKP RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF SERINE HYDROXYMETHYLTRANSFERASECOMPLEXED WITH
REMARK 900 SERINE
REMARK 900 RELATED ID: 1KL1 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF SERINE HYDROXYMETHYLTRANSFERASECOMPLEXED WITH
REMARK 900 GLYCINE
REMARK 900 RELATED ID: 1YJY RELATED DB: PDB
REMARK 900 K226M MUTANT OF SERINE HYDROXYMETHYLTRANSFERASE FROM
REMARK 900 B.STEAROTHERMOPHILUS, COMPLEX WITH SERINE
REMARK 900 RELATED ID: 1YJZ RELATED DB: PDB
REMARK 900 K226M MUTANT OF SERINE HYDROXYMETHYLTRANSFERASE FROM
REMARK 900 B.STEAROTHERMOPHILUS
REMARK 900 RELATED ID: 2VGS RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF E53QBSSHMT INTERNAL ALDIMINE
REMARK 900 RELATED ID: 2VGU RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF E53QBSSHMT WITH L- SERINE
REMARK 900 RELATED ID: 2VI8 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF S172ABSSHMT INTERNAL ALDIMINE
REMARK 900 RELATED ID: 2VI9 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF S172ABSSHMT GLYCINE EXTERNAL ALDIMINE
REMARK 900 RELATED ID: 2VIA RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF S172ABSSHMT L-SERINE EXTERNAL ALDIMINE
DBREF 2VIB A 1 405 UNP Q7SIB6 Q7SIB6_BACST 1 405
SEQADV 2VIB ALA A 172 UNP Q7SIB6 SER 172 ENGINEERED MUTATION
SEQRES 1 A 405 MET LYS TYR LEU PRO GLN GLN ASP PRO GLN VAL PHE ALA
SEQRES 2 A 405 ALA ILE GLU GLN GLU ARG LYS ARG GLN HIS ALA LYS ILE
SEQRES 3 A 405 GLU LEU ILE ALA SER GLU ASN PHE VAL SER ARG ALA VAL
SEQRES 4 A 405 MET GLU ALA GLN GLY SER VAL LEU THR ASN LYS TYR ALA
SEQRES 5 A 405 GLU GLY TYR PRO GLY ARG ARG TYR TYR GLY GLY CYS GLU
SEQRES 6 A 405 TYR VAL ASP ILE VAL GLU GLU LEU ALA ARG GLU ARG ALA
SEQRES 7 A 405 LYS GLN LEU PHE GLY ALA GLU HIS ALA ASN VAL GLN PRO
SEQRES 8 A 405 HIS SER GLY ALA GLN ALA ASN MET ALA VAL TYR PHE THR
SEQRES 9 A 405 VAL LEU GLU HIS GLY ASP THR VAL LEU GLY MET ASN LEU
SEQRES 10 A 405 SER HIS GLY GLY HIS LEU THR HIS GLY SER PRO VAL ASN
SEQRES 11 A 405 PHE SER GLY VAL GLN TYR ASN PHE VAL ALA TYR GLY VAL
SEQRES 12 A 405 ASP PRO GLU THR HIS VAL ILE ASP TYR ASP ASP VAL ARG
SEQRES 13 A 405 GLU LYS ALA ARG LEU HIS ARG PRO LYS LEU ILE VAL ALA
SEQRES 14 A 405 ALA ALA ALA ALA TYR PRO ARG ILE ILE ASP PHE ALA LYS
SEQRES 15 A 405 PHE ARG GLU ILE ALA ASP GLU VAL GLY ALA TYR LEU MET
SEQRES 16 A 405 VAL ASP MET ALA HIS ILE ALA GLY LEU VAL ALA ALA GLY
SEQRES 17 A 405 LEU HIS PRO ASN PRO VAL PRO TYR ALA HIS PHE VAL THR
SEQRES 18 A 405 THR THR THR HIS LYS THR LEU ARG GLY PRO ARG GLY GLY
SEQRES 19 A 405 MET ILE LEU CYS GLN GLU GLN PHE ALA LYS GLN ILE ASP
SEQRES 20 A 405 LYS ALA ILE PHE PRO GLY ILE GLN GLY GLY PRO LEU MET
SEQRES 21 A 405 HIS VAL ILE ALA ALA LYS ALA VAL ALA PHE GLY GLU ALA
SEQRES 22 A 405 LEU GLN ASP ASP PHE LYS ALA TYR ALA LYS ARG VAL VAL
SEQRES 23 A 405 ASP ASN ALA LYS ARG LEU ALA SER ALA LEU GLN ASN GLU
SEQRES 24 A 405 GLY PHE THR LEU VAL SER GLY GLY THR ASP ASN HIS LEU
SEQRES 25 A 405 LEU LEU VAL ASP LEU ARG PRO GLN GLN LEU THR GLY LYS
SEQRES 26 A 405 THR ALA GLU LYS VAL LEU ASP GLU VAL GLY ILE THR VAL
SEQRES 27 A 405 ASN LYS ASN THR ILE PRO TYR ASP PRO GLU SER PRO PHE
SEQRES 28 A 405 VAL THR SER GLY ILE ARG ILE GLY THR ALA ALA VAL THR
SEQRES 29 A 405 THR ARG GLY PHE GLY LEU GLU GLU MET ASP GLU ILE ALA
SEQRES 30 A 405 ALA ILE ILE GLY LEU VAL LEU LYS ASN VAL GLY SER GLU
SEQRES 31 A 405 GLN ALA LEU GLU GLU ALA ARG GLN ARG VAL ALA ALA LEU
SEQRES 32 A 405 THR ASP
HET GLY A1407 5
HET PLP A1406 15
HET MPD A1408 8
HET MPD A1409 8
HET PO4 A1410 5
HETNAM GLY GLYCINE
HETNAM PLP PYRIDOXAL-5'-PHOSPHATE
HETNAM MPD (4S)-2-METHYL-2,4-PENTANEDIOL
HETNAM PO4 PHOSPHATE ION
HETSYN PLP VITAMIN B6 PHOSPHATE
FORMUL 2 GLY C2 H5 N O2
FORMUL 3 PLP C8 H10 N O6 P
FORMUL 4 MPD 2(C6 H14 O2)
FORMUL 6 PO4 O4 P 3-
FORMUL 7 HOH *415(H2 O)
HELIX 1 1 TYR A 3 ASP A 8 1 6
HELIX 2 2 ASP A 8 LYS A 25 1 18
HELIX 3 3 SER A 36 GLY A 44 1 9
HELIX 4 4 SER A 45 LYS A 50 5 6
HELIX 5 5 CYS A 64 GLY A 83 1 20
HELIX 6 6 SER A 93 LEU A 106 1 14
HELIX 7 7 LEU A 117 GLY A 120 5 4
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 ILE A 201 ALA A 207 1 7
HELIX 12 12 GLN A 239 PHE A 251 1 13
HELIX 13 13 LEU A 259 LEU A 274 1 16
HELIX 14 14 GLN A 275 GLU A 299 1 25
HELIX 15 15 SER A 305 GLY A 307 5 3
HELIX 16 16 ARG A 318 GLN A 321 5 4
HELIX 17 17 THR A 323 VAL A 334 1 12
HELIX 18 18 THR A 360 ARG A 366 1 7
HELIX 19 19 GLY A 369 LYS A 385 1 17
HELIX 20 20 SER A 389 ASP A 405 1 17
SHEET 1 AA 2 ILE A 26 GLU A 27 0
SHEET 2 AA 2 ILE A 336 THR A 337 1 N THR A 337 O ILE A 26
SHEET 1 AB 2 GLY A 54 TYR A 55 0
SHEET 2 AB 2 ARG A 58 ARG A 59 -1 O ARG A 58 N TYR A 55
SHEET 1 AC 7 HIS A 86 ASN A 88 0
SHEET 2 AC 7 GLY A 234 CYS A 238 -1 O ILE A 236 N ASN A 88
SHEET 3 AC 7 PHE A 219 THR A 223 -1 O VAL A 220 N LEU A 237
SHEET 4 AC 7 TYR A 193 ASP A 197 1 O LEU A 194 N PHE A 219
SHEET 5 AC 7 LEU A 166 ALA A 169 1 O ILE A 167 N MET A 195
SHEET 6 AC 7 THR A 111 MET A 115 1 O LEU A 113 N VAL A 168
SHEET 7 AC 7 ASN A 137 TYR A 141 1 O ASN A 137 N VAL A 112
SHEET 1 AD 4 THR A 302 LEU A 303 0
SHEET 2 AD 4 LEU A 312 ASP A 316 -1 O ASP A 316 N THR A 302
SHEET 3 AD 4 GLY A 355 GLY A 359 -1 O ILE A 356 N VAL A 315
SHEET 4 AD 4 ASN A 339 LYS A 340 -1 O ASN A 339 N ARG A 357
LINK C4A PLP A1406 N GLY A1407 1555 1555 1.24
CISPEP 1 PHE A 251 PRO A 252 0 9.18
SITE 1 AC1 19 TYR A 51 SER A 93 GLY A 94 ALA A 95
SITE 2 AC1 19 HIS A 122 ALA A 171 ALA A 172 ASP A 197
SITE 3 AC1 19 ALA A 199 HIS A 200 THR A 223 HIS A 225
SITE 4 AC1 19 LYS A 226 GLY A 256 GLY A 257 GLY A1407
SITE 5 AC1 19 HOH A2080 HOH A2410 HOH A2411
SITE 1 AC2 8 SER A 31 TYR A 51 TYR A 61 HIS A 122
SITE 2 AC2 8 HIS A 200 LYS A 226 ARG A 357 PLP A1406
SITE 1 AC3 9 TYR A 152 ARG A 156 GLN A 321 LEU A 322
SITE 2 AC3 9 VAL A 387 HOH A2229 HOH A2326 HOH A2412
SITE 3 AC3 9 HOH A2413
SITE 1 AC4 3 PHE A 131 GLN A 135 TYR A 136
SITE 1 AC5 4 GLU A 371 GLU A 375 HOH A2372 HOH A2414
CRYST1 61.240 106.330 57.206 90.00 90.00 90.00 P 21 21 2 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 0.016329 0.000000 0.000000 0.00000
SCALE2 0.000000 0.009405 0.000000 0.00000
SCALE3 0.000000 0.000000 0.017481 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
