HEADER OXIDOREDUCTASE 15-MAR-11 3R33
TITLE EVIDENCE FOR DYNAMIC MOTION IN PROTEINS AS A MECHANISM FOR LIGAND
TITLE 2 DISSOCIATION
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DIHYDROFOLATE REDUCTASE;
COMPND 3 CHAIN: A;
COMPND 4 EC: 1.5.1.3
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI K-12;
SOURCE 3 ORGANISM_TAXID: 83333;
SOURCE 4 STRAIN: K12
KEYWDS ROSSMANN FOLD, REDUCTASE, OXIDOREDUCTASE
EXPDTA X-RAY DIFFRACTION
AUTHOR E.J.COLLINS,A.L.LEE,M.J.CARROLL,R.V.MAULDIN,A.V.GROMOVA,S.F.SINGLETON
REVDAT 4 21-FEB-24 3R33 1 REMARK SEQADV LINK
REVDAT 3 12-NOV-14 3R33 1 KEYWDS
REVDAT 2 25-APR-12 3R33 1 JRNL
REVDAT 1 25-JAN-12 3R33 0
JRNL AUTH M.J.CARROLL,R.V.MAULDIN,A.V.GROMOVA,S.F.SINGLETON,
JRNL AUTH 2 E.J.COLLINS,A.L.LEE
JRNL TITL EVIDENCE FOR DYNAMICS IN PROTEINS AS A MECHANISM FOR LIGAND
JRNL TITL 2 DISSOCIATION.
JRNL REF NAT.CHEM.BIOL. V. 8 246 2012
JRNL REFN ISSN 1552-4450
JRNL PMID 22246400
JRNL DOI 10.1038/NCHEMBIO.769
REMARK 2
REMARK 2 RESOLUTION. 2.09 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : BUSTER 2.8.0
REMARK 3 AUTHORS : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER,
REMARK 3 : PACIOREK,ROVERSI,SHARFF,SMART,VONRHEIN,
REMARK 3 : WOMACK,MATTHEWS,TEN EYCK,TRONRUD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.09
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 15.32
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : NULL
REMARK 3 NUMBER OF REFLECTIONS : 9261
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) : 0.185
REMARK 3 R VALUE (WORKING SET) : 0.181
REMARK 3 FREE R VALUE : 0.245
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.900
REMARK 3 FREE R VALUE TEST SET COUNT : 454
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 : 5
REMARK 3 BIN RESOLUTION RANGE HIGH (ANGSTROMS) : 2.09
REMARK 3 BIN RESOLUTION RANGE LOW (ANGSTROMS) : 2.34
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 REFLECTIONS IN BIN (WORKING + TEST SET) : 2602
REMARK 3 BIN R VALUE (WORKING + TEST SET) : 0.1888
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 2470
REMARK 3 BIN R VALUE (WORKING SET) : 0.1841
REMARK 3 BIN FREE R VALUE : 0.2774
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5.07
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 132
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 : 1268
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 81
REMARK 3 SOLVENT ATOMS : 177
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 13.55
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 10.84
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.70970
REMARK 3 B22 (A**2) : 0.92760
REMARK 3 B33 (A**2) : -0.21780
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) : 0.226
REMARK 3 DPI (BLOW EQ-10) BASED ON R VALUE (A) : NULL
REMARK 3 DPI (BLOW EQ-9) BASED ON FREE R VALUE (A) : NULL
REMARK 3 DPI (CRUICKSHANK) BASED ON R VALUE (A) : NULL
REMARK 3 DPI (CRUICKSHANK) BASED ON FREE R VALUE (A) : NULL
REMARK 3
REMARK 3 REFERENCES: BLOW, D. (2002) ACTA CRYST D58, 792-797
REMARK 3 CRUICKSHANK, D.W.J. (1999) ACTA CRYST D55, 583-601
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.928
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.881
REMARK 3
REMARK 3 NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15
REMARK 3 TERM COUNT WEIGHT FUNCTION.
REMARK 3 BOND LENGTHS : 1453 ; 2.000 ; NULL
REMARK 3 BOND ANGLES : 2003 ; 2.000 ; NULL
REMARK 3 TORSION ANGLES : 487 ; 2.000 ; NULL
REMARK 3 TRIGONAL CARBON PLANES : 39 ; 2.000 ; NULL
REMARK 3 GENERAL PLANES : 212 ; 5.000 ; NULL
REMARK 3 ISOTROPIC THERMAL FACTORS : 1387 ; 20.000 ; NULL
REMARK 3 BAD NON-BONDED CONTACTS : 10 ; 5.000 ; NULL
REMARK 3 IMPROPER TORSIONS : NULL ; NULL ; NULL
REMARK 3 PSEUDOROTATION ANGLES : NULL ; NULL ; NULL
REMARK 3 CHIRAL IMPROPER TORSION : 187 ; 5.000 ; NULL
REMARK 3 SUM OF OCCUPANCIES : NULL ; NULL ; NULL
REMARK 3 UTILITY DISTANCES : NULL ; NULL ; NULL
REMARK 3 UTILITY ANGLES : NULL ; NULL ; NULL
REMARK 3 UTILITY TORSION : NULL ; NULL ; NULL
REMARK 3 IDEAL-DIST CONTACT TERM : 1789 ; 4.000 ; NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.010
REMARK 3 BOND ANGLES (DEGREES) : 1.16
REMARK 3 PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 3.11
REMARK 3 OTHER TORSION ANGLES (DEGREES) : 17.11
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 1
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: { A|* }
REMARK 3 ORIGIN FOR THE GROUP (A): 6.4329 -1.5864 -12.9948
REMARK 3 T TENSOR
REMARK 3 T11: -0.0784 T22: -0.0284
REMARK 3 T33: -0.0743 T12: -0.0034
REMARK 3 T13: 0.0116 T23: 0.0138
REMARK 3 L TENSOR
REMARK 3 L11: 0.4801 L22: 1.0319
REMARK 3 L33: 0.8738 L12: 0.0887
REMARK 3 L13: -0.0201 L23: 0.4147
REMARK 3 S TENSOR
REMARK 3 S11: -0.0137 S12: 0.0501 S13: 0.0233
REMARK 3 S21: 0.0713 S22: 0.0316 S23: 0.0489
REMARK 3 S31: -0.0661 S32: -0.0357 S33: -0.0179
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 3R33 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 07-APR-11.
REMARK 100 THE DEPOSITION ID IS D_1000064427.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 11-MAY-09
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.0
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 RU300
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.54
REMARK 200 MONOCHROMATOR : VARIMAX HF
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : RIGAKU SATURN 944+
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 9261
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.090
REMARK 200 RESOLUTION RANGE LOW (A) : 15.320
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.3
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) : 2.09
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.20
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.9
REMARK 200 DATA REDUNDANCY IN SHELL : 3.70
REMARK 200 R MERGE FOR SHELL (I) : 0.05500
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: PHASER
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 41.07
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.09
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 20 MG/ML DHFR, 20 MM IMIDAZOLE, 300 MM
REMARK 280 CACL2, 30% PEG-6000, PH 8.0, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 298K
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 17.06500
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 48.86000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 22.55500
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 48.86000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 17.06500
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 22.55500
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 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 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 173 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 11 OD2
REMARK 620 2 HOH A 253 O 112.1
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 165 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 SER A 49 OG
REMARK 620 2 NDP A1160 O2D 109.8
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 180 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ARG A 52 O
REMARK 620 2 ARG A 52 O 0.9
REMARK 620 3 HOH A 296 O 146.0 145.1
REMARK 620 4 HOH A 346 O 126.3 127.1 83.6
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 169 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ILE A 82 O
REMARK 620 2 GLY A 86 O 123.8
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 170 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 101 OE1
REMARK 620 2 HOH A 225 O 103.6
REMARK 620 3 HOH A 258 O 79.5 127.4
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 160 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 116 OD1
REMARK 620 2 HOH A 307 O 126.2
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 178 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 122 O
REMARK 620 2 HOH A 259 O 106.2
REMARK 620 3 HOH A 301 O 68.2 74.1
REMARK 620 4 HOH A 318 O 59.3 105.3 125.2
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 174 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 131 OD1
REMARK 620 2 HOH A 327 O 102.0
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 166 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 134 OE1
REMARK 620 2 HOH A 247 O 119.8
REMARK 620 N 1
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 6ME A 161
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NDP A 1160
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 160
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 162
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 163
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 164
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 165
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 166
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 167
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 168
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 169
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 170
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 171
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 172
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 173
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 174
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 175
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 176
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 177
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 178
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 179
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 180
DBREF 3R33 A 1 159 UNP P0ABQ4 DYR_ECOLI 1 159
SEQADV 3R33 ASP A 37 UNP P0ABQ4 ASN 37 CONFLICT
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 ASP LYS PRO
SEQRES 4 A 159 VAL ILE MET GLY ARG HIS THR TRP GLU SER ILE GLY ARG
SEQRES 5 A 159 PRO LEU 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 CYS 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 CYS PHE GLU ILE LEU
SEQRES 13 A 159 GLU ARG ARG
HET 6ME A 161 13
HET NDP A1160 48
HET CA A 160 1
HET CL A 162 1
HET CA A 163 1
HET CA A 164 1
HET CA A 165 1
HET CA A 166 1
HET CA A 167 1
HET CA A 168 1
HET CA A 169 1
HET CA A 170 1
HET CA A 171 1
HET CA A 172 1
HET CA A 173 1
HET CA A 174 1
HET CA A 175 1
HET CL A 176 1
HET CL A 177 1
HET CA A 178 1
HET CA A 179 1
HET CA A 180 1
HETNAM 6ME (6S)-6-METHYL-5,6,7,8-TETRAHYDROQUINAZOLINE-2,4-DIAMINE
HETNAM NDP NADPH DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE
HETNAM 2 NDP PHOSPHATE
HETNAM CA CALCIUM ION
HETNAM CL CHLORIDE ION
FORMUL 2 6ME C9 H14 N4
FORMUL 3 NDP C21 H30 N7 O17 P3
FORMUL 4 CA 17(CA 2+)
FORMUL 5 CL 3(CL 1-)
FORMUL 24 HOH *177(H2 O)
HELIX 1 1 ALA A 9 ASP A 11 5 3
HELIX 2 2 LEU A 24 LEU A 36 1 13
HELIX 3 3 ARG A 44 GLY A 51 1 8
HELIX 4 4 SER A 77 ALA A 84 1 8
HELIX 5 5 GLY A 96 LEU A 104 1 9
HELIX 6 6 PRO A 105 ALA A 107 5 3
HELIX 7 7 GLU A 129 ASP A 131 5 3
SHEET 1 A 8 THR A 73 VAL A 75 0
SHEET 2 A 8 ASN A 59 LEU A 62 1 N ILE A 61 O THR A 73
SHEET 3 A 8 VAL A 40 GLY A 43 1 N VAL A 40 O ILE A 60
SHEET 4 A 8 ILE A 91 VAL A 93 1 O MET A 92 N ILE A 41
SHEET 5 A 8 ILE A 2 LEU A 8 1 N SER A 3 O VAL A 93
SHEET 6 A 8 LYS A 109 ILE A 115 1 O ILE A 115 N LEU A 8
SHEET 7 A 8 TYR A 151 ARG A 158 -1 O GLU A 154 N LEU A 112
SHEET 8 A 8 TRP A 133 HIS A 141 -1 N VAL A 136 O ILE A 155
SHEET 1 B 2 VAL A 13 GLY A 15 0
SHEET 2 B 2 THR A 123 HIS A 124 -1 O THR A 123 N ILE A 14
LINK OD2 ASP A 11 CA CA A 173 1555 1555 3.01
LINK OG ASER A 49 CA CA A 165 1555 1555 3.09
LINK O BARG A 52 CA CA A 180 1555 1555 2.62
LINK O AARG A 52 CA CA A 180 1555 1555 2.66
LINK O ILE A 82 CA CA A 169 1555 1555 2.48
LINK O GLY A 86 CA CA A 169 1555 1555 2.60
LINK OE1 GLU A 101 CA CA A 170 1555 1555 2.31
LINK OD1 ASP A 116 CA CA A 160 1555 1555 2.63
LINK O ASP A 116 CA CA A 168 1555 1555 2.26
LINK O ASP A 122 CA CA A 178 1555 1555 2.78
LINK OD1 ASP A 127 CA CA A 175 1555 1555 3.00
LINK OD1 ASP A 131 CA CA A 174 1555 1555 2.51
LINK OE1 GLU A 134 CA CA A 166 1555 1555 2.48
LINK CA CA A 160 O HOH A 307 1555 1555 2.63
LINK CA CA A 163 O2X NDP A1160 1555 1555 2.72
LINK CA CA A 164 O HOH A 305 1555 1555 2.96
LINK CA CA A 165 O2D NDP A1160 1555 1555 3.10
LINK CA CA A 166 O HOH A 247 1555 1555 2.60
LINK CA CA A 167 O HOH A 326 1555 1555 2.13
LINK CA CA A 170 O HOH A 225 1555 1555 3.04
LINK CA CA A 170 O HOH A 258 1555 1555 2.78
LINK CA CA A 172 O HOH A 249 1555 1555 2.44
LINK CA CA A 173 O HOH A 253 1555 1555 2.39
LINK CA CA A 174 O HOH A 327 1555 1555 2.46
LINK CA CA A 178 O HOH A 259 1555 1555 2.90
LINK CA CA A 178 O HOH A 301 1555 1555 2.72
LINK CA CA A 178 O HOH A 318 1555 1555 2.81
LINK CA CA A 179 O HOH A 285 1555 1555 2.54
LINK CA CA A 180 O HOH A 296 1555 1555 2.48
LINK CA CA A 180 O HOH A 346 1555 1555 2.35
CISPEP 1 GLY A 95 GLY A 96 0 -2.01
SITE 1 AC1 8 ILE A 5 ALA A 6 ASP A 27 PHE A 31
SITE 2 AC1 8 ILE A 94 TYR A 100 THR A 113 HOH A 214
SITE 1 AC2 34 ALA A 6 ALA A 7 ILE A 14 GLY A 15
SITE 2 AC2 34 ASN A 18 ALA A 19 MET A 20 TRP A 22
SITE 3 AC2 34 GLY A 43 ARG A 44 HIS A 45 THR A 46
SITE 4 AC2 34 LEU A 62 SER A 63 SER A 64 LYS A 76
SITE 5 AC2 34 ILE A 94 GLY A 96 GLY A 97 ARG A 98
SITE 6 AC2 34 VAL A 99 TYR A 100 GLN A 102 THR A 123
SITE 7 AC2 34 ASP A 131 CA A 163 CA A 165 HOH A 212
SITE 8 AC2 34 HOH A 228 HOH A 241 HOH A 252 HOH A 257
SITE 9 AC2 34 HOH A 286 HOH A 311
SITE 1 AC3 4 VAL A 10 ASP A 116 HOH A 307 HOH A 356
SITE 1 AC4 8 ASP A 116 HIS A 149 SER A 150 CA A 168
SITE 2 AC4 8 CL A 177 HOH A 181 HOH A 204 HOH A 247
SITE 1 AC5 3 ARG A 44 GLN A 65 NDP A1160
SITE 1 AC6 4 ARG A 52 PRO A 53 GLU A 80 HOH A 305
SITE 1 AC7 3 MET A 20 SER A 49 NDP A1160
SITE 1 AC8 3 GLU A 134 GLU A 157 HOH A 247
SITE 1 AC9 4 PRO A 105 LYS A 106 HOH A 278 HOH A 326
SITE 1 BC1 7 ASP A 116 HIS A 149 ARG A 159 CL A 162
SITE 2 BC1 7 CL A 177 HOH A 247 HOH A 258
SITE 1 BC2 3 ILE A 82 GLY A 86 HOH A 226
SITE 1 BC3 5 GLU A 101 ARG A 159 CL A 177 HOH A 225
SITE 2 BC3 5 HOH A 258
SITE 1 BC4 2 ALA A 19 MET A 20
SITE 1 BC5 5 GLY A 121 HIS A 124 PHE A 140 CYS A 152
SITE 2 BC5 5 HOH A 249
SITE 1 BC6 2 ASP A 11 HOH A 253
SITE 1 BC7 4 VAL A 78 ASP A 79 ASP A 131 HOH A 327
SITE 1 BC8 3 ARG A 12 ASP A 127 TYR A 128
SITE 1 BC9 3 LYS A 32 PRO A 55 ARG A 57
SITE 1 CC1 8 GLU A 101 ASP A 116 ARG A 159 CL A 162
SITE 2 CC1 8 CA A 168 CA A 170 HOH A 258 HOH A 307
SITE 1 CC2 5 ASP A 116 ASP A 122 HOH A 259 HOH A 301
SITE 2 CC2 5 HOH A 318
SITE 1 CC3 1 HOH A 285
SITE 1 CC4 3 ARG A 52 HOH A 296 HOH A 346
CRYST1 34.130 45.110 97.720 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 0.029300 0.000000 0.000000 0.00000
SCALE2 0.000000 0.022168 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010233 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
