HEADER OXIDOREDUCTASE 03-SEP-09 3IX9
TITLE CRYSTAL STRUCTURE OF STREPTOCOCCUS PNEUMONIAE DIHYDROFOLATE REDUCTASE
TITLE 2 - SP9 MUTANT
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DIHYDROFOLATE REDUCTASE;
COMPND 3 CHAIN: A, B;
COMPND 4 EC: 1.5.1.3;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: STREPTOCOCCUS PNEUMONIAE;
SOURCE 3 ORGANISM_TAXID: 1313;
SOURCE 4 GENE: DFR;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: ER2566, DTHYDFOL;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET28A
KEYWDS CENTRAL BETA SHEET SURROUNDED BY 4 ALPHA HELICES, OXIDOREDUCTASE
EXPDTA X-RAY DIFFRACTION
AUTHOR N.H.YENNAWAR
REVDAT 3 06-SEP-23 3IX9 1 REMARK
REVDAT 2 13-OCT-21 3IX9 1 REMARK SEQADV
REVDAT 1 02-FEB-10 3IX9 0
JRNL AUTH J.LEE,N.H.YENNAWAR,J.GAM,S.J.BENKOVIC
JRNL TITL KINETIC AND STRUCTURAL CHARACTERIZATION OF DIHYDROFOLATE
JRNL TITL 2 REDUCTASE FROM STREPTOCOCCUS PNEUMONIAE
JRNL REF BIOCHEMISTRY V. 49 195 2010
JRNL REFN ISSN 0006-2960
JRNL PMID 19950924
JRNL DOI 10.1021/BI901614M
REMARK 2
REMARK 2 RESOLUTION. 1.95 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.2
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) : 1.95
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.00
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) (%) : 92.6
REMARK 3 NUMBER OF REFLECTIONS : 28610
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING SET) : 0.237
REMARK 3 FREE R VALUE : 0.274
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.600
REMARK 3 FREE R VALUE TEST SET COUNT : 1424
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 : 2750
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 162
REMARK 3 SOLVENT ATOMS : 306
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 8.18200
REMARK 3 B22 (A**2) : -3.60000
REMARK 3 B33 (A**2) : -4.58100
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 COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM SIGMAA (A) : NULL
REMARK 3 LOW RESOLUTION CUTOFF (A) : NULL
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM C-V SIGMAA (A) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.010
REMARK 3 BOND ANGLES (DEGREES) : 1.520
REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL
REMARK 3 IMPROPER ANGLES (DEGREES) : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : 2.521 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 3.232 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 3.577 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 4.484 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : NULL
REMARK 3 KSOL : 0.45
REMARK 3 BSOL : 74.38
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 3IX9 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 04-SEP-09.
REMARK 100 THE DEPOSITION ID IS D_1000054979.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-JUL-08
REMARK 200 TEMPERATURE (KELVIN) : 93
REMARK 200 PH : 4.0
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 MICROMAX-007 HF
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : RIGAKU SATURN 944+
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : CRYSTALCLEAR
REMARK 200 DATA SCALING SOFTWARE : CRYSTALCLEAR
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 28610
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.950
REMARK 200 RESOLUTION RANGE LOW (A) : 40.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 92.6
REMARK 200 DATA REDUNDANCY : 2.340
REMARK 200 R MERGE (I) : 0.10200
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 5.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.95
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.02
REMARK 200 COMPLETENESS FOR SHELL (%) : 92.6
REMARK 200 DATA REDUNDANCY IN SHELL : 1.41
REMARK 200 R MERGE FOR SHELL (I) : 0.21000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.400
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: PDB ENTRY 1ZDR
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 47.07
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.32
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1M LITHIUM CHLORIDE, 0.1M SODIUM
REMARK 280 CITRATE PH 4.0, 20% PEG 6000, VAPOR DIFFUSION, SITTING DROP,
REMARK 280 TEMPERATURE 298K
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 30.91900
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 46.81950
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 30.91900
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 46.81950
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3
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 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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
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
REMARK 350 BIOMOLECULE: 3
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH A 209 LIES ON A SPECIAL POSITION.
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 -19
REMARK 465 LYS A -18
REMARK 465 HIS A -17
REMARK 465 HIS A -16
REMARK 465 HIS A -15
REMARK 465 HIS A -14
REMARK 465 HIS A -13
REMARK 465 HIS A -12
REMARK 465 HIS A -11
REMARK 465 HIS A -10
REMARK 465 GLY A -9
REMARK 465 GLY A -8
REMARK 465 LEU A -7
REMARK 465 VAL A -6
REMARK 465 PRO A -5
REMARK 465 ARG A -4
REMARK 465 GLY A -3
REMARK 465 SER A -2
REMARK 465 HIS A -1
REMARK 465 GLY A 0
REMARK 465 MET A 1
REMARK 465 VAL A 168
REMARK 465 LEU A 169
REMARK 465 GLU A 170
REMARK 465 MET B -19
REMARK 465 LYS B -18
REMARK 465 HIS B -17
REMARK 465 HIS B -16
REMARK 465 HIS B -15
REMARK 465 HIS B -14
REMARK 465 HIS B -13
REMARK 465 HIS B -12
REMARK 465 HIS B -11
REMARK 465 HIS B -10
REMARK 465 GLY B -9
REMARK 465 GLY B -8
REMARK 465 LEU B -7
REMARK 465 VAL B -6
REMARK 465 PRO B -5
REMARK 465 ARG B -4
REMARK 465 GLY B -3
REMARK 465 SER B -2
REMARK 465 HIS B -1
REMARK 465 GLY B 0
REMARK 465 MET B 1
REMARK 465 VAL B 168
REMARK 465 LEU B 169
REMARK 465 GLU B 170
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 THR A 2 OG1 CG2
REMARK 470 THR B 2 OG1 CG2
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
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,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
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 ATM2 ATM3
REMARK 500 GLY B 102 N - CA - C ANGL. DEV. = -15.3 DEGREES
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 GLU A 71 127.31 -39.22
REMARK 500 ILE A 74 -99.37 -131.45
REMARK 500 ASP A 75 -138.60 -104.43
REMARK 500 SER A 144 162.89 179.78
REMARK 500 LYS A 166 -169.53 -79.38
REMARK 500 PRO B 24 42.96 -75.86
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 NDP A 193
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MTX A 200
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NDP B 193
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MTX B 200
DBREF 3IX9 A 1 168 UNP O85261 O85261_STRPN 1 168
DBREF 3IX9 B 1 168 UNP O85261 O85261_STRPN 1 168
SEQADV 3IX9 MET A -19 UNP O85261 EXPRESSION TAG
SEQADV 3IX9 LYS A -18 UNP O85261 EXPRESSION TAG
SEQADV 3IX9 HIS A -17 UNP O85261 EXPRESSION TAG
SEQADV 3IX9 HIS A -16 UNP O85261 EXPRESSION TAG
SEQADV 3IX9 HIS A -15 UNP O85261 EXPRESSION TAG
SEQADV 3IX9 HIS A -14 UNP O85261 EXPRESSION TAG
SEQADV 3IX9 HIS A -13 UNP O85261 EXPRESSION TAG
SEQADV 3IX9 HIS A -12 UNP O85261 EXPRESSION TAG
SEQADV 3IX9 HIS A -11 UNP O85261 EXPRESSION TAG
SEQADV 3IX9 HIS A -10 UNP O85261 EXPRESSION TAG
SEQADV 3IX9 GLY A -9 UNP O85261 EXPRESSION TAG
SEQADV 3IX9 GLY A -8 UNP O85261 EXPRESSION TAG
SEQADV 3IX9 LEU A -7 UNP O85261 EXPRESSION TAG
SEQADV 3IX9 VAL A -6 UNP O85261 EXPRESSION TAG
SEQADV 3IX9 PRO A -5 UNP O85261 EXPRESSION TAG
SEQADV 3IX9 ARG A -4 UNP O85261 EXPRESSION TAG
SEQADV 3IX9 GLY A -3 UNP O85261 EXPRESSION TAG
SEQADV 3IX9 SER A -2 UNP O85261 EXPRESSION TAG
SEQADV 3IX9 HIS A -1 UNP O85261 EXPRESSION TAG
SEQADV 3IX9 GLY A 0 UNP O85261 EXPRESSION TAG
SEQADV 3IX9 TYR A 26 UNP O85261 HIS 26 ENGINEERED MUTATION
SEQADV 3IX9 LYS A 60 UNP O85261 GLN 60 ENGINEERED MUTATION
SEQADV 3IX9 VAL A 77 UNP O85261 ALA 77 ENGINEERED MUTATION
SEQADV 3IX9 ALA A 78 UNP O85261 VAL 78 ENGINEERED MUTATION
SEQADV 3IX9 HIS A 81 UNP O85261 GLN 81 ENGINEERED MUTATION
SEQADV 3IX9 SER A 91 UNP O85261 GLN 91 ENGINEERED MUTATION
SEQADV 3IX9 VAL A 100 UNP O85261 LEU 100 ENGINEERED MUTATION
SEQADV 3IX9 ALA A 133 UNP O85261 GLU 133 ENGINEERED MUTATION
SEQADV 3IX9 THR A 149 UNP O85261 ALA 149 ENGINEERED MUTATION
SEQADV 3IX9 LEU A 169 UNP O85261 EXPRESSION TAG
SEQADV 3IX9 GLU A 170 UNP O85261 EXPRESSION TAG
SEQADV 3IX9 MET B -19 UNP O85261 EXPRESSION TAG
SEQADV 3IX9 LYS B -18 UNP O85261 EXPRESSION TAG
SEQADV 3IX9 HIS B -17 UNP O85261 EXPRESSION TAG
SEQADV 3IX9 HIS B -16 UNP O85261 EXPRESSION TAG
SEQADV 3IX9 HIS B -15 UNP O85261 EXPRESSION TAG
SEQADV 3IX9 HIS B -14 UNP O85261 EXPRESSION TAG
SEQADV 3IX9 HIS B -13 UNP O85261 EXPRESSION TAG
SEQADV 3IX9 HIS B -12 UNP O85261 EXPRESSION TAG
SEQADV 3IX9 HIS B -11 UNP O85261 EXPRESSION TAG
SEQADV 3IX9 HIS B -10 UNP O85261 EXPRESSION TAG
SEQADV 3IX9 GLY B -9 UNP O85261 EXPRESSION TAG
SEQADV 3IX9 GLY B -8 UNP O85261 EXPRESSION TAG
SEQADV 3IX9 LEU B -7 UNP O85261 EXPRESSION TAG
SEQADV 3IX9 VAL B -6 UNP O85261 EXPRESSION TAG
SEQADV 3IX9 PRO B -5 UNP O85261 EXPRESSION TAG
SEQADV 3IX9 ARG B -4 UNP O85261 EXPRESSION TAG
SEQADV 3IX9 GLY B -3 UNP O85261 EXPRESSION TAG
SEQADV 3IX9 SER B -2 UNP O85261 EXPRESSION TAG
SEQADV 3IX9 HIS B -1 UNP O85261 EXPRESSION TAG
SEQADV 3IX9 GLY B 0 UNP O85261 EXPRESSION TAG
SEQADV 3IX9 TYR B 26 UNP O85261 HIS 26 ENGINEERED MUTATION
SEQADV 3IX9 LYS B 60 UNP O85261 GLN 60 ENGINEERED MUTATION
SEQADV 3IX9 VAL B 77 UNP O85261 ALA 77 ENGINEERED MUTATION
SEQADV 3IX9 ALA B 78 UNP O85261 VAL 78 ENGINEERED MUTATION
SEQADV 3IX9 HIS B 81 UNP O85261 GLN 81 ENGINEERED MUTATION
SEQADV 3IX9 SER B 91 UNP O85261 GLN 91 ENGINEERED MUTATION
SEQADV 3IX9 VAL B 100 UNP O85261 LEU 100 ENGINEERED MUTATION
SEQADV 3IX9 ALA B 133 UNP O85261 GLU 133 ENGINEERED MUTATION
SEQADV 3IX9 THR B 149 UNP O85261 ALA 149 ENGINEERED MUTATION
SEQADV 3IX9 LEU B 169 UNP O85261 EXPRESSION TAG
SEQADV 3IX9 GLU B 170 UNP O85261 EXPRESSION TAG
SEQRES 1 A 190 MET LYS HIS HIS HIS HIS HIS HIS HIS HIS GLY GLY LEU
SEQRES 2 A 190 VAL PRO ARG GLY SER HIS GLY MET THR LYS LYS ILE VAL
SEQRES 3 A 190 ALA ILE TRP ALA GLN ASP GLU GLU GLY VAL ILE GLY LYS
SEQRES 4 A 190 ASP ASN ARG LEU PRO TRP TYR LEU PRO ALA GLU LEU GLN
SEQRES 5 A 190 HIS PHE LYS GLU THR THR LEU ASN HIS ALA ILE LEU MET
SEQRES 6 A 190 GLY ARG VAL THR PHE ASP GLY MET GLY ARG ARG LEU LEU
SEQRES 7 A 190 PRO LYS ARG GLU THR LEU ILE LEU THR ARG ASN PRO GLU
SEQRES 8 A 190 GLU LYS ILE ASP GLY VAL ALA THR PHE HIS ASP VAL GLN
SEQRES 9 A 190 SER VAL LEU ASP TRP TYR SER ALA GLN GLU LYS ASN LEU
SEQRES 10 A 190 TYR ILE VAL GLY GLY LYS GLN ILE PHE GLN ALA PHE GLU
SEQRES 11 A 190 PRO TYR LEU ASP GLU VAL ILE VAL THR HIS ILE HIS ALA
SEQRES 12 A 190 ARG VAL GLU GLY ASP THR TYR PHE PRO ALA GLU PHE ASP
SEQRES 13 A 190 LEU SER LEU PHE GLU THR VAL SER SER LYS PHE TYR THR
SEQRES 14 A 190 LYS ASP GLU LYS ASN PRO TYR ASP PHE THR ILE GLN TYR
SEQRES 15 A 190 ARG LYS ARG LYS GLU VAL LEU GLU
SEQRES 1 B 190 MET LYS HIS HIS HIS HIS HIS HIS HIS HIS GLY GLY LEU
SEQRES 2 B 190 VAL PRO ARG GLY SER HIS GLY MET THR LYS LYS ILE VAL
SEQRES 3 B 190 ALA ILE TRP ALA GLN ASP GLU GLU GLY VAL ILE GLY LYS
SEQRES 4 B 190 ASP ASN ARG LEU PRO TRP TYR LEU PRO ALA GLU LEU GLN
SEQRES 5 B 190 HIS PHE LYS GLU THR THR LEU ASN HIS ALA ILE LEU MET
SEQRES 6 B 190 GLY ARG VAL THR PHE ASP GLY MET GLY ARG ARG LEU LEU
SEQRES 7 B 190 PRO LYS ARG GLU THR LEU ILE LEU THR ARG ASN PRO GLU
SEQRES 8 B 190 GLU LYS ILE ASP GLY VAL ALA THR PHE HIS ASP VAL GLN
SEQRES 9 B 190 SER VAL LEU ASP TRP TYR SER ALA GLN GLU LYS ASN LEU
SEQRES 10 B 190 TYR ILE VAL GLY GLY LYS GLN ILE PHE GLN ALA PHE GLU
SEQRES 11 B 190 PRO TYR LEU ASP GLU VAL ILE VAL THR HIS ILE HIS ALA
SEQRES 12 B 190 ARG VAL GLU GLY ASP THR TYR PHE PRO ALA GLU PHE ASP
SEQRES 13 B 190 LEU SER LEU PHE GLU THR VAL SER SER LYS PHE TYR THR
SEQRES 14 B 190 LYS ASP GLU LYS ASN PRO TYR ASP PHE THR ILE GLN TYR
SEQRES 15 B 190 ARG LYS ARG LYS GLU VAL LEU GLU
HET NDP A 193 48
HET MTX A 200 33
HET NDP B 193 48
HET MTX B 200 33
HETNAM NDP NADPH DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE
HETNAM 2 NDP PHOSPHATE
HETNAM MTX METHOTREXATE
FORMUL 3 NDP 2(C21 H30 N7 O17 P3)
FORMUL 4 MTX 2(C20 H22 N8 O5)
FORMUL 7 HOH *306(H2 O)
HELIX 1 1 LEU A 27 LEU A 39 1 13
HELIX 2 2 ARG A 47 MET A 53 1 7
HELIX 3 3 ASP A 82 ALA A 92 1 11
HELIX 4 4 GLY A 102 GLU A 110 1 9
HELIX 5 5 PRO A 111 LEU A 113 5 3
HELIX 6 6 ASP A 136 SER A 138 5 3
HELIX 7 7 LEU B 27 LEU B 39 1 13
HELIX 8 8 ARG B 47 MET B 53 1 7
HELIX 9 9 ASP B 82 ALA B 92 1 11
HELIX 10 10 GLY B 102 GLU B 110 1 9
HELIX 11 11 PRO B 111 LEU B 113 5 3
HELIX 12 12 ASP B 136 SER B 138 5 3
SHEET 1 A 8 ALA A 78 PHE A 80 0
SHEET 2 A 8 GLU A 62 LEU A 66 1 N ILE A 65 O ALA A 78
SHEET 3 A 8 ALA A 42 GLY A 46 1 N ILE A 43 O LEU A 64
SHEET 4 A 8 LEU A 97 GLY A 101 1 O TYR A 98 N LEU A 44
SHEET 5 A 8 ILE A 5 GLN A 11 1 N VAL A 6 O LEU A 97
SHEET 6 A 8 GLU A 115 ILE A 121 1 O THR A 119 N TRP A 9
SHEET 7 A 8 PHE A 158 ARG A 165 -1 O THR A 159 N HIS A 120
SHEET 8 A 8 PHE A 140 TYR A 148 -1 N SER A 144 O TYR A 162
SHEET 1 B 2 VAL A 16 GLY A 18 0
SHEET 2 B 2 THR A 129 TYR A 130 -1 O THR A 129 N ILE A 17
SHEET 1 C 8 ALA B 78 PHE B 80 0
SHEET 2 C 8 GLU B 62 LEU B 66 1 N ILE B 65 O ALA B 78
SHEET 3 C 8 ALA B 42 GLY B 46 1 N ILE B 43 O LEU B 64
SHEET 4 C 8 LEU B 97 GLY B 101 1 O TYR B 98 N LEU B 44
SHEET 5 C 8 ILE B 5 GLN B 11 1 N VAL B 6 O ILE B 99
SHEET 6 C 8 GLU B 115 ILE B 121 1 O ILE B 121 N GLN B 11
SHEET 7 C 8 PHE B 158 ARG B 165 -1 O THR B 159 N HIS B 120
SHEET 8 C 8 PHE B 140 TYR B 148 -1 N VAL B 143 O TYR B 162
SHEET 1 D 2 VAL B 16 GLY B 18 0
SHEET 2 D 2 THR B 129 TYR B 130 -1 O THR B 129 N ILE B 17
SITE 1 AC1 32 TRP A 9 ALA A 10 ILE A 17 GLY A 18
SITE 2 AC1 32 ASN A 21 ARG A 22 LEU A 23 GLY A 46
SITE 3 AC1 32 ARG A 47 VAL A 48 THR A 49 LEU A 66
SITE 4 AC1 32 THR A 67 ARG A 68 HIS A 81 VAL A 100
SITE 5 AC1 32 GLY A 101 GLY A 102 LYS A 103 GLN A 104
SITE 6 AC1 32 ILE A 105 HOH A 176 HOH A 182 MTX A 200
SITE 7 AC1 32 HOH A 208 HOH A 222 HOH A 270 HOH A 275
SITE 8 AC1 32 HOH A 277 HOH A 281 HOH A 297 HOH A 308
SITE 1 AC2 17 ILE A 8 TRP A 9 LEU A 23 GLU A 30
SITE 2 AC2 17 GLN A 32 PHE A 34 LYS A 35 ARG A 61
SITE 3 AC2 17 VAL A 100 HOH A 187 HOH A 190 HOH A 192
SITE 4 AC2 17 NDP A 193 HOH A 206 HOH A 207 HOH A 215
SITE 5 AC2 17 HOH A 330
SITE 1 AC3 35 ASN A 40 HOH A 185 HOH A 210 HOH A 218
SITE 2 AC3 35 TRP B 9 ALA B 10 ILE B 17 GLY B 18
SITE 3 AC3 35 LYS B 19 ASN B 21 ARG B 22 LEU B 23
SITE 4 AC3 35 TRP B 25 GLY B 46 ARG B 47 VAL B 48
SITE 5 AC3 35 THR B 49 LEU B 66 THR B 67 ARG B 68
SITE 6 AC3 35 HIS B 81 VAL B 100 GLY B 101 GLY B 102
SITE 7 AC3 35 LYS B 103 GLN B 104 ILE B 105 HOH B 182
SITE 8 AC3 35 HOH B 187 HOH B 197 MTX B 200 HOH B 205
SITE 9 AC3 35 HOH B 231 HOH B 246 HOH B 277
SITE 1 AC4 18 HOH A 280 ILE B 8 TRP B 9 LEU B 23
SITE 2 AC4 18 PRO B 28 GLU B 30 LEU B 31 GLN B 32
SITE 3 AC4 18 PHE B 34 LYS B 35 ARG B 56 ARG B 61
SITE 4 AC4 18 VAL B 100 THR B 119 HOH B 188 NDP B 193
SITE 5 AC4 18 HOH B 236 HOH B 244
CRYST1 61.838 93.639 71.367 90.00 90.00 90.00 P 21 21 2 8
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 0.016171 0.000000 0.000000 0.00000
SCALE2 0.000000 0.010679 0.000000 0.00000
SCALE3 0.000000 0.000000 0.014012 0.00000
(ATOM LINES ARE NOT SHOWN.)
END