HEADER OXIDOREDUCTASE 22-MAR-14 4P68
TITLE ELECTROSTATICS OF ACTIVE SITE MICROENVIRONMENTS FOR E. COLI DHFR
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DIHYDROFOLATE REDUCTASE;
COMPND 3 CHAIN: A;
COMPND 4 EC: 1.5.1.3;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 562;
SOURCE 4 GENE: FOLA, ECS0051, LF82_0721;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS ELECTROSTATICS, CATALYSIS, OXIDOREDUCTASE, DHFR
EXPDTA X-RAY DIFFRACTION
AUTHOR C.T.LIU,J.P.LAYFIELD,R.J.STEWART III,J.B.FRENCH,P.HANOIAN,J.B.ASBURY,
AUTHOR 2 S.HAMMES-SCHIFFER,S.J.BENKOVIC
REVDAT 6 27-DEC-23 4P68 1 REMARK LINK
REVDAT 5 25-DEC-19 4P68 1 REMARK
REVDAT 4 20-SEP-17 4P68 1 SOURCE REMARK
REVDAT 3 01-OCT-14 4P68 1 JRNL
REVDAT 2 06-AUG-14 4P68 1 AUTHOR
REVDAT 1 16-JUL-14 4P68 0
JRNL AUTH C.T.LIU,J.P.LAYFIELD,R.J.STEWART,J.B.FRENCH,P.HANOIAN,
JRNL AUTH 2 J.B.ASBURY,S.HAMMES-SCHIFFER,S.J.BENKOVIC
JRNL TITL PROBING THE ELECTROSTATICS OF ACTIVE SITE MICROENVIRONMENTS
JRNL TITL 2 ALONG THE CATALYTIC CYCLE FOR ESCHERICHIA COLI DIHYDROFOLATE
JRNL TITL 3 REDUCTASE.
JRNL REF J.AM.CHEM.SOC. V. 136 10349 2014
JRNL REFN ESSN 1520-5126
JRNL PMID 24977791
JRNL DOI 10.1021/JA5038947
REMARK 2
REMARK 2 RESOLUTION. 2.26 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0110
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) : 2.26
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 25.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 95.1
REMARK 3 NUMBER OF REFLECTIONS : 6821
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) : 0.194
REMARK 3 R VALUE (WORKING SET) : 0.191
REMARK 3 FREE R VALUE : 0.251
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.700
REMARK 3 FREE R VALUE TEST SET COUNT : 320
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) : 2.26
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.32
REMARK 3 REFLECTION IN BIN (WORKING SET) : 426
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 88.13
REMARK 3 BIN R VALUE (WORKING SET) : 0.2210
REMARK 3 BIN FREE R VALUE SET COUNT : 12
REMARK 3 BIN FREE R VALUE : 0.2660
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1234
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 91
REMARK 3 SOLVENT ATOMS : 39
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 25.54
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.37000
REMARK 3 B22 (A**2) : 0.78000
REMARK 3 B33 (A**2) : -0.40000
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): 0.510
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.268
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.191
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 7.664
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.946
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.913
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 1361 ; 0.016 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): 877 ; 0.005 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 1856 ; 1.593 ; 2.015
REMARK 3 BOND ANGLES OTHERS (DEGREES): 2131 ; 1.107 ; 3.019
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 156 ; 5.790 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 56 ;37.282 ;23.929
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 194 ;17.329 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 7 ;10.783 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 199 ; 0.099 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1480 ; 0.008 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 270 ; 0.002 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
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): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
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): 807 ; 0.863 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 321 ; 0.148 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 1288 ; 1.623 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 554 ; 2.210 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 568 ; 3.658 ; 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 U VALUES: REFINED INDIVIDUALLY
REMARK 4
REMARK 4 4P68 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 25-MAR-14.
REMARK 100 THE DEPOSITION ID IS D_1000200790.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 09-JUN-13
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : CHESS
REMARK 200 BEAMLINE : A1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.978
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 210
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 6821
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.260
REMARK 200 RESOLUTION RANGE LOW (A) : 49.290
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 95.9
REMARK 200 DATA REDUNDANCY : 5.100
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 15.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
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: MOLREP
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 38.34
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.99
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 50 MM CALCIUM ACETATE, 34% PEG 400,
REMARK 280 100 MM HEPES, PH 6.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE
REMARK 280 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
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 17.06600
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 49.29300
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 21.32500
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 49.29300
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 17.06600
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 21.32500
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: MONOMERIC
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 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 GLU A 17 CG CD OE1 OE2
REMARK 470 ASN A 23 CG OD1 ND2
REMARK 470 LEU A 28 CG CD1 CD2
REMARK 470 ARG A 33 CD NE CZ NH1 NH2
REMARK 470 ARG A 52 CZ NH1 NH2
REMARK 470 GLN A 108 CG CD OE1 NE2
REMARK 470 GLU A 118 CD OE1 OE2
REMARK 470 GLU A 129 CG CD OE1 OE2
REMARK 470 GLU A 134 CG CD OE1 OE2
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 XCN A 54 O - C - N ANGL. DEV. = -15.1 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 ALA A 9 -153.41 -110.60
REMARK 500 ASP A 69 119.24 -160.45
REMARK 500 ASP A 144 -152.92 -143.53
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY
REMARK 500
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 500 I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI ANGLE
REMARK 500 XCN A 54 26.29
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 205 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 116 O
REMARK 620 2 ARG A 159 OXT 18.0
REMARK 620 3 HOH A 306 O 21.6 4.2
REMARK 620 4 HOH A 324 O 25.6 7.6 5.3
REMARK 620 N 1 2 3
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MTX A 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue NAP A 202
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ACT A 203
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ACT A 204
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CA A 205
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4P66 RELATED DB: PDB
REMARK 900 4P66 CONTAINS THE SAME PROTEIN WITH THE NITRILE PROBE INSTALLED AT
REMARK 900 A DIFFERENT POSITION
DBREF 4P68 A 1 159 UNP C3TR70 C3TR70_ECOLX 1 159
SEQADV 4P68 XCN A 54 UNP C3TR70 LEU 54 ENGINEERED MUTATION
SEQADV 4P68 ALA A 85 UNP C3TR70 CYS 85 ENGINEERED MUTATION
SEQADV 4P68 SER A 152 UNP C3TR70 CYS 152 ENGINEERED MUTATION
SEQRES 1 A 159 MET ILE SER LEU ILE ALA ALA LEU ALA VAL ASP ARG VAL
SEQRES 2 A 159 ILE GLY MET GLU ASN ALA MET PRO TRP ASN LEU PRO ALA
SEQRES 3 A 159 ASP LEU ALA TRP PHE LYS ARG ASN THR LEU ASN LYS PRO
SEQRES 4 A 159 VAL ILE MET GLY ARG HIS THR TRP GLU SER ILE GLY ARG
SEQRES 5 A 159 PRO XCN PRO GLY ARG LYS ASN ILE ILE LEU SER SER GLN
SEQRES 6 A 159 PRO GLY THR ASP ASP ARG VAL THR TRP VAL LYS SER VAL
SEQRES 7 A 159 ASP GLU ALA ILE ALA ALA ALA GLY ASP VAL PRO GLU ILE
SEQRES 8 A 159 MET VAL ILE GLY GLY GLY ARG VAL TYR GLU GLN PHE LEU
SEQRES 9 A 159 PRO LYS ALA GLN LYS LEU TYR LEU THR HIS ILE ASP ALA
SEQRES 10 A 159 GLU VAL GLU GLY ASP THR HIS PHE PRO ASP TYR GLU PRO
SEQRES 11 A 159 ASP ASP TRP GLU SER VAL PHE SER GLU PHE HIS ASP ALA
SEQRES 12 A 159 ASP ALA GLN ASN SER HIS SER TYR SER PHE GLU ILE LEU
SEQRES 13 A 159 GLU ARG ARG
HET XCN A 54 8
HET MTX A 201 33
HET NAP A 202 48
HET ACT A 203 4
HET ACT A 204 4
HET CA A 205 1
HET CA A 206 1
HETNAM XCN S-CYANO-L-CYSTEINE
HETNAM MTX METHOTREXATE
HETNAM NAP NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE
HETNAM ACT ACETATE ION
HETNAM CA CALCIUM ION
HETSYN NAP 2'-MONOPHOSPHOADENOSINE 5'-DIPHOSPHORIBOSE
FORMUL 1 XCN C4 H6 N2 O2 S
FORMUL 2 MTX C20 H22 N8 O5
FORMUL 3 NAP C21 H28 N7 O17 P3
FORMUL 4 ACT 2(C2 H3 O2 1-)
FORMUL 6 CA 2(CA 2+)
FORMUL 8 HOH *39(H2 O)
HELIX 1 AA1 ALA A 9 ASP A 11 5 3
HELIX 2 AA2 LEU A 24 LEU A 36 1 13
HELIX 3 AA3 ARG A 44 GLY A 51 1 8
HELIX 4 AA4 SER A 77 ALA A 85 1 9
HELIX 5 AA5 GLY A 96 LEU A 104 1 9
HELIX 6 AA6 PRO A 105 ALA A 107 5 3
SHEET 1 AA1 8 THR A 73 VAL A 75 0
SHEET 2 AA1 8 ASN A 59 LEU A 62 1 N ASN A 59 O THR A 73
SHEET 3 AA1 8 VAL A 40 GLY A 43 1 N MET A 42 O LEU A 62
SHEET 4 AA1 8 ILE A 91 GLY A 95 1 O ILE A 94 N ILE A 41
SHEET 5 AA1 8 ILE A 2 LEU A 8 1 N SER A 3 O VAL A 93
SHEET 6 AA1 8 LYS A 109 ILE A 115 1 O ILE A 115 N LEU A 8
SHEET 7 AA1 8 TYR A 151 ARG A 158 -1 O GLU A 154 N LEU A 112
SHEET 8 AA1 8 TRP A 133 HIS A 141 -1 N HIS A 141 O TYR A 151
SHEET 1 AA2 2 VAL A 13 GLY A 15 0
SHEET 2 AA2 2 THR A 123 HIS A 124 -1 O THR A 123 N ILE A 14
LINK C PRO A 53 N XCN A 54 1555 1555 1.27
LINK C XCN A 54 N PRO A 55 1555 1555 1.30
LINK O ASP A 116 CA CA A 205 1555 1655 2.45
LINK OXT ARG A 159 CA CA A 205 1555 1555 2.73
LINK CA CA A 205 O HOH A 306 1555 3454 2.17
LINK CA CA A 205 O HOH A 324 1555 1455 2.07
CISPEP 1 GLY A 95 GLY A 96 0 -0.61
SITE 1 AC1 13 ILE A 5 ALA A 6 ALA A 7 MET A 20
SITE 2 AC1 13 ASP A 27 PHE A 31 ILE A 50 XCN A 54
SITE 3 AC1 13 ARG A 57 ILE A 94 TYR A 100 NAP A 202
SITE 4 AC1 13 HOH A 328
SITE 1 AC2 28 ALA A 6 ALA A 7 ILE A 14 ASN A 18
SITE 2 AC2 28 ALA A 19 MET A 20 GLY A 43 ARG A 44
SITE 3 AC2 28 HIS A 45 THR A 46 LEU A 62 SER A 63
SITE 4 AC2 28 SER A 64 GLN A 65 LYS A 76 ILE A 94
SITE 5 AC2 28 GLY A 96 GLY A 97 ARG A 98 VAL A 99
SITE 6 AC2 28 TYR A 100 GLN A 102 ASP A 131 GLU A 139
SITE 7 AC2 28 MTX A 201 HOH A 303 HOH A 315 HOH A 333
SITE 1 AC3 2 ASP A 70 ASP A 87
SITE 1 AC4 1 ASP A 70
SITE 1 AC5 5 ASP A 116 HIS A 149 ARG A 159 HOH A 306
SITE 2 AC5 5 HOH A 324
CRYST1 34.132 42.650 98.586 90.00 90.00 90.00 P 21 21 21 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 0.029298 0.000000 0.000000 0.00000
SCALE2 0.000000 0.023447 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010143 0.00000
(ATOM LINES ARE NOT SHOWN.)
END