HEADER OXIDOREDUCTASE 02-JUN-11 3SA1
TITLE BACUILLS ANTHRACIS DIHYDROFOLATE REDUCTASE BOUND PROPARGYL-LINKED TMP
TITLE 2 ANALOG, UCP1021
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: BACILLUS ANTHRACIS;
SOURCE 3 ORGANISM_COMMON: ANTHRAX,ANTHRAX BACTERIUM;
SOURCE 4 ORGANISM_TAXID: 1392;
SOURCE 5 GENE: BAS2083, BA_2237, DFRA, GBAA2237, GBAA_2237;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 1007065;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: M15;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PQE2
KEYWDS OXIDOREDUCTASE
EXPDTA X-RAY DIFFRACTION
AUTHOR A.C.ANDERSON,J.M.BEIERLEIN
REVDAT 2 13-SEP-23 3SA1 1 REMARK SEQADV
REVDAT 1 13-JUN-12 3SA1 0
JRNL AUTH A.C.ANDERSON,J.M.BEIERLEIN,K.VISWANATHAN,D.L.WRIGHT
JRNL TITL SAR STUDIES OF HETEROCYCLIC PROPARGYL-LINKED TMP ANALOGS TO
JRNL TITL 2 BACILLUS DIHYDROFOLATE REDUCTASE
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.50 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0109
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) : 2.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 42.63
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.1
REMARK 3 NUMBER OF REFLECTIONS : 13963
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) : 0.230
REMARK 3 R VALUE (WORKING SET) : 0.229
REMARK 3 FREE R VALUE : 0.257
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 699
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) : 2.50
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.57
REMARK 3 REFLECTION IN BIN (WORKING SET) : 966
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 98.55
REMARK 3 BIN R VALUE (WORKING SET) : 0.2710
REMARK 3 BIN FREE R VALUE SET COUNT : 53
REMARK 3 BIN FREE R VALUE : 0.3470
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 : 150
REMARK 3 SOLVENT ATOMS : 35
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 30.79
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): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.309
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.214
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 9.460
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.918
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.887
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 3011 ; 0.010 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 4093 ; 1.337 ; 2.002
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 333 ; 6.113 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 155 ;37.242 ;24.000
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 497 ;15.306 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 16 ;11.501 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 409 ; 0.087 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2320 ; 0.005 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
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): 1646 ; 0.565 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2678 ; 1.076 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1365 ; 1.281 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1412 ; 2.156 ; 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 : 1
REMARK 3
REMARK 3 NCS GROUP NUMBER : 1
REMARK 3 CHAIN NAMES : A B
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 13
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 1 A 10 3
REMARK 3 1 B 1 B 10 3
REMARK 3 2 A 25 A 29 3
REMARK 3 2 B 25 B 29 3
REMARK 3 3 A 31 A 32 3
REMARK 3 3 B 31 B 32 3
REMARK 3 4 A 35 A 36 3
REMARK 3 4 B 35 B 36 3
REMARK 3 5 A 38 A 71 3
REMARK 3 5 B 38 B 71 3
REMARK 3 6 A 73 A 81 3
REMARK 3 6 B 73 B 81 3
REMARK 3 7 A 83 A 87 3
REMARK 3 7 B 83 B 87 3
REMARK 3 8 A 89 A 90 3
REMARK 3 8 B 89 B 90 3
REMARK 3 9 A 92 A 128 3
REMARK 3 9 B 92 B 128 3
REMARK 3 10 A 137 A 146 3
REMARK 3 10 B 137 B 146 3
REMARK 3 11 A 149 A 160 3
REMARK 3 11 B 149 B 160 3
REMARK 3 12 A 20 A 23 3
REMARK 3 12 B 20 B 23 3
REMARK 3 13 A 12 A 18 3
REMARK 3 13 B 12 B 18 3
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT POSITIONAL 1 A (A): 555 ; 0.030 ; 0.050
REMARK 3 LOOSE POSITIONAL 1 A (A): 584 ; 0.040 ; 5.000
REMARK 3 TIGHT THERMAL 1 A (A**2): 555 ; 0.080 ; 0.500
REMARK 3 LOOSE THERMAL 1 A (A**2): 584 ; 0.080 ;10.000
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 3SA1 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 08-JUN-11.
REMARK 100 THE DEPOSITION ID IS D_1000065949.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 13-DEC-10
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
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 : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS IV++
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : D*TREK
REMARK 200 DATA SCALING SOFTWARE : D*TREK 9.9.8.8L, SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 13990
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.500
REMARK 200 RESOLUTION RANGE LOW (A) : 42.630
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 5.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.3
REMARK 200 DATA REDUNDANCY : 3.200
REMARK 200 R MERGE (I) : 0.13800
REMARK 200 R SYM (I) : 0.13800
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 5.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.50
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.57
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.6
REMARK 200 DATA REDUNDANCY IN SHELL : 3.30
REMARK 200 R MERGE FOR SHELL (I) : 0.38300
REMARK 200 R SYM FOR SHELL (I) : 0.38300
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 3E0B
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 52.83
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.61
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: INITIAL CRYSTAL HITS WERE GROWN IN
REMARK 280 27.5% (W/V) PEG 10,000, 0.1 M MES, PH 6.50, AT AN EQUAL RATIO OF
REMARK 280 PROTEIN TO CRYSTALLIZATION SOLUTION. MICROSEEDING WAS USED TO
REMARK 280 OBTAIN ISOLATED CRYSTALS IN 10% (W/V) PEG 10,000 AND 0.1 MES, PH
REMARK 280 6.50 AT A PROTEIN CONCENTRATION OF 5 MG/ML, VAPOR DIFFUSION,
REMARK 280 HANGING DROP, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 42
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 -Y,X,Z+1/2
REMARK 290 4555 Y,-X,Z+1/2
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 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 33.53500
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 33.53500
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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 350
REMARK 350 BIOMOLECULE: 2
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: 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 HIS A -2
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAP A 207
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 6DR A 163
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAP B 207
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 6DR B 163
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3SA2 RELATED DB: PDB
REMARK 900 RELATED ID: 3SAI RELATED DB: PDB
REMARK 900 RELATED ID: 3E0B RELATED DB: PDB
REMARK 900 RELATED ID: 3S9U RELATED DB: PDB
REMARK 900 RELATED ID: 3JVX RELATED DB: PDB
REMARK 900 RELATED ID: 3JWM RELATED DB: PDB
REMARK 900 RELATED ID: 3JWC RELATED DB: PDB
REMARK 900 RELATED ID: 3JWF RELATED DB: PDB
DBREF 3SA1 A 1 162 UNP Q81R22 Q81R22_BACAN 1 162
DBREF 3SA1 B 1 162 UNP Q81R22 Q81R22_BACAN 1 162
SEQADV 3SA1 HIS A -2 UNP Q81R22 EXPRESSION TAG
SEQADV 3SA1 HIS A -1 UNP Q81R22 EXPRESSION TAG
SEQADV 3SA1 HIS A 0 UNP Q81R22 EXPRESSION TAG
SEQADV 3SA1 ARG A 2 UNP Q81R22 ILE 2 ENGINEERED MUTATION
SEQADV 3SA1 HIS B -2 UNP Q81R22 EXPRESSION TAG
SEQADV 3SA1 HIS B -1 UNP Q81R22 EXPRESSION TAG
SEQADV 3SA1 HIS B 0 UNP Q81R22 EXPRESSION TAG
SEQADV 3SA1 ARG B 2 UNP Q81R22 ILE 2 ENGINEERED MUTATION
SEQRES 1 A 165 HIS HIS HIS MET ARG VAL SER PHE MET VAL ALA MET ASP
SEQRES 2 A 165 GLU ASN ARG VAL ILE GLY LYS ASP ASN ASN LEU PRO TRP
SEQRES 3 A 165 ARG LEU PRO SER GLU LEU GLN TYR VAL LYS LYS THR THR
SEQRES 4 A 165 MET GLY HIS PRO LEU ILE MET GLY ARG LYS ASN TYR GLU
SEQRES 5 A 165 ALA ILE GLY ARG PRO LEU PRO GLY ARG ARG ASN ILE ILE
SEQRES 6 A 165 VAL THR ARG ASN GLU GLY TYR HIS VAL GLU GLY CYS GLU
SEQRES 7 A 165 VAL ALA HIS SER VAL GLU GLU VAL PHE GLU LEU CYS LYS
SEQRES 8 A 165 ASN GLU GLU GLU ILE PHE ILE PHE GLY GLY ALA GLN ILE
SEQRES 9 A 165 TYR ASP LEU PHE LEU PRO TYR VAL ASP LYS LEU TYR ILE
SEQRES 10 A 165 THR LYS ILE HIS HIS ALA PHE GLU GLY ASP THR PHE PHE
SEQRES 11 A 165 PRO GLU MET ASP MET THR ASN TRP LYS GLU VAL PHE VAL
SEQRES 12 A 165 GLU LYS GLY LEU THR ASP GLU LYS ASN PRO TYR THR TYR
SEQRES 13 A 165 TYR TYR HIS VAL TYR GLU LYS GLN GLN
SEQRES 1 B 165 HIS HIS HIS MET ARG VAL SER PHE MET VAL ALA MET ASP
SEQRES 2 B 165 GLU ASN ARG VAL ILE GLY LYS ASP ASN ASN LEU PRO TRP
SEQRES 3 B 165 ARG LEU PRO SER GLU LEU GLN TYR VAL LYS LYS THR THR
SEQRES 4 B 165 MET GLY HIS PRO LEU ILE MET GLY ARG LYS ASN TYR GLU
SEQRES 5 B 165 ALA ILE GLY ARG PRO LEU PRO GLY ARG ARG ASN ILE ILE
SEQRES 6 B 165 VAL THR ARG ASN GLU GLY TYR HIS VAL GLU GLY CYS GLU
SEQRES 7 B 165 VAL ALA HIS SER VAL GLU GLU VAL PHE GLU LEU CYS LYS
SEQRES 8 B 165 ASN GLU GLU GLU ILE PHE ILE PHE GLY GLY ALA GLN ILE
SEQRES 9 B 165 TYR ASP LEU PHE LEU PRO TYR VAL ASP LYS LEU TYR ILE
SEQRES 10 B 165 THR LYS ILE HIS HIS ALA PHE GLU GLY ASP THR PHE PHE
SEQRES 11 B 165 PRO GLU MET ASP MET THR ASN TRP LYS GLU VAL PHE VAL
SEQRES 12 B 165 GLU LYS GLY LEU THR ASP GLU LYS ASN PRO TYR THR TYR
SEQRES 13 B 165 TYR TYR HIS VAL TYR GLU LYS GLN GLN
HET NAP A 207 48
HET 6DR A 163 27
HET NAP B 207 48
HET 6DR B 163 27
HETNAM NAP NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE
HETNAM 6DR 6-ETHYL-5-{3-[2-METHOXY-5-(PYRIDIN-4-YL)PHENYL]PROP-1-
HETNAM 2 6DR YN-1-YL}PYRIMIDINE-2,4-DIAMINE
HETSYN NAP 2'-MONOPHOSPHOADENOSINE 5'-DIPHOSPHORIBOSE
FORMUL 3 NAP 2(C21 H28 N7 O17 P3)
FORMUL 4 6DR 2(C21 H21 N5 O)
FORMUL 7 HOH *35(H2 O)
HELIX 1 1 LEU A 25 MET A 37 1 13
HELIX 2 2 ARG A 45 GLY A 52 1 8
HELIX 3 3 SER A 79 CYS A 87 1 9
HELIX 4 4 GLY A 98 LEU A 106 1 9
HELIX 5 5 PRO A 107 VAL A 109 5 3
HELIX 6 6 LEU B 25 MET B 37 1 13
HELIX 7 7 ARG B 45 GLY B 52 1 8
HELIX 8 8 SER B 79 CYS B 87 1 9
HELIX 9 9 GLY B 98 LEU B 106 1 9
HELIX 10 10 PRO B 107 VAL B 109 5 3
SHEET 1 A16 GLU A 75 ALA A 77 0
SHEET 2 A16 ASN A 60 VAL A 63 1 N ASN A 60 O GLU A 75
SHEET 3 A16 LEU A 41 GLY A 44 1 N MET A 43 O ILE A 61
SHEET 4 A16 GLU A 92 ILE A 95 1 O PHE A 94 N ILE A 42
SHEET 5 A16 ARG A 2 ASP A 10 1 N SER A 4 O ILE A 95
SHEET 6 A16 LYS A 111 ILE A 117 1 O ILE A 117 N MET A 9
SHEET 7 A16 TYR A 153 LYS A 160 -1 O TYR A 158 N LEU A 112
SHEET 8 A16 TRP A 135 LYS A 142 -1 N GLU A 141 O TYR A 155
SHEET 9 A16 TRP B 135 LYS B 142 1 O VAL B 140 N GLU A 137
SHEET 10 A16 TYR B 153 LYS B 160 -1 O TYR B 155 N GLU B 141
SHEET 11 A16 LYS B 111 ILE B 117 -1 N LEU B 112 O TYR B 158
SHEET 12 A16 ARG B 2 ASP B 10 1 N PHE B 5 O TYR B 113
SHEET 13 A16 GLU B 92 ILE B 95 1 O ILE B 95 N SER B 4
SHEET 14 A16 LEU B 41 GLY B 44 1 N ILE B 42 O PHE B 94
SHEET 15 A16 ASN B 60 VAL B 63 1 O ILE B 61 N MET B 43
SHEET 16 A16 GLU B 75 ALA B 77 1 O GLU B 75 N ASN B 60
SHEET 1 B 2 VAL A 14 GLY A 16 0
SHEET 2 B 2 THR A 125 PHE A 126 -1 O THR A 125 N ILE A 15
SHEET 1 C 2 VAL B 14 GLY B 16 0
SHEET 2 C 2 THR B 125 PHE B 126 -1 O THR B 125 N ILE B 15
CISPEP 1 GLY A 97 GLY A 98 0 2.26
CISPEP 2 GLY B 97 GLY B 98 0 4.17
SITE 1 AC1 25 VAL A 7 ALA A 8 ILE A 15 ASN A 19
SITE 2 AC1 25 ASN A 20 LEU A 21 GLY A 44 ARG A 45
SITE 3 AC1 25 LYS A 46 ASN A 47 VAL A 63 THR A 64
SITE 4 AC1 25 ARG A 65 HIS A 78 PHE A 96 GLY A 97
SITE 5 AC1 25 GLY A 98 ALA A 99 GLN A 100 ILE A 101
SITE 6 AC1 25 TYR A 102 LEU A 104 6DR A 163 HOH A 164
SITE 7 AC1 25 HOH A 169
SITE 1 AC2 15 MET A 6 VAL A 7 ALA A 8 ASN A 20
SITE 2 AC2 15 LEU A 21 GLU A 28 VAL A 32 LYS A 33
SITE 3 AC2 15 ASN A 47 ALA A 50 ARG A 53 LEU A 55
SITE 4 AC2 15 PHE A 96 HOH A 169 NAP A 207
SITE 1 AC3 27 VAL B 7 ALA B 8 ILE B 15 GLY B 16
SITE 2 AC3 27 ASN B 19 ASN B 20 LEU B 21 TRP B 23
SITE 3 AC3 27 GLY B 44 ARG B 45 LYS B 46 ASN B 47
SITE 4 AC3 27 VAL B 63 THR B 64 ARG B 65 HIS B 78
SITE 5 AC3 27 PHE B 96 GLY B 97 GLY B 98 ALA B 99
SITE 6 AC3 27 GLN B 100 ILE B 101 TYR B 102 LEU B 104
SITE 7 AC3 27 6DR B 163 HOH B 171 HOH B 172
SITE 1 AC4 12 MET B 6 VAL B 7 ALA B 8 LEU B 21
SITE 2 AC4 12 TRP B 23 GLU B 28 VAL B 32 ASN B 47
SITE 3 AC4 12 ALA B 50 ILE B 51 PHE B 96 NAP B 207
CRYST1 78.094 78.094 67.070 90.00 90.00 90.00 P 42 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 0.012805 0.000000 0.000000 0.00000
SCALE2 0.000000 0.012805 0.000000 0.00000
SCALE3 0.000000 0.000000 0.014910 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
