HEADER HYDROLASE/HYDROLASE INHIBITOR 02-JUL-18 6DYY
TITLE CRYSTAL STRUCTURE OF HELICOBACTER PYLORI 5'-METHYLTHIOADENOSINE/S-
TITLE 2 ADENOSYL HOMOCYSTEINE NUCLEOSIDASE (MTAN) COMPLEXED WITH (3R,4S)-1-
TITLE 3 ((4-AMINO-5H-PYRROLO[3,2-D]PYRIMIDIN-7-YL)METHYL)-4-(((3-(1-BUTYL-1H-
TITLE 4 1,2,3-TRIAZOL-4-YL)PROPYL)THIO)METHYL)PYRROLIDIN-3-OL
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: 5'-METHYLTHIOADENOSINE/S-ADENOSYLHOMOCYSTEINE NUCLEOSIDASE;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 EC: 3.2.2.9;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HELICOBACTER PYLORI;
SOURCE 3 ORGANISM_COMMON: CAMPYLOBACTER PYLORI;
SOURCE 4 ORGANISM_TAXID: 210;
SOURCE 5 GENE: BW246_00770, BZL55_04980, CEP79_03920;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS MTAN ENZYME, DUODENAL ULCERS, STOMACH CANCER, HYDROLASE-HYDROLASE
KEYWDS 2 INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR R.K.HARIJAN,R.G.DUCATI,J.B.BONANNO,S.C.ALMO,V.L.SCHRAMM
REVDAT 4 11-OCT-23 6DYY 1 LINK
REVDAT 3 24-APR-19 6DYY 1 JRNL
REVDAT 2 10-APR-19 6DYY 1 JRNL
REVDAT 1 20-MAR-19 6DYY 0
JRNL AUTH R.K.HARIJAN,O.HOFF,R.G.DUCATI,R.S.FIRESTONE,B.M.HIRSCH,
JRNL AUTH 2 G.B.EVANS,V.L.SCHRAMM,P.C.TYLER
JRNL TITL SELECTIVE INHIBITORS OF HELICOBACTER PYLORI
JRNL TITL 2 METHYLTHIOADENOSINE NUCLEOSIDASE AND HUMAN
JRNL TITL 3 METHYLTHIOADENOSINE PHOSPHORYLASE.
JRNL REF J. MED. CHEM. V. 62 3286 2019
JRNL REFN ISSN 1520-4804
JRNL PMID 30860833
JRNL DOI 10.1021/ACS.JMEDCHEM.8B01642
REMARK 2
REMARK 2 RESOLUTION. 1.61 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0189
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) : 1.61
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 88.44
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 117541
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) : 0.180
REMARK 3 R VALUE (WORKING SET) : 0.179
REMARK 3 FREE R VALUE : 0.203
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 6265
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) : 1.61
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.65
REMARK 3 REFLECTION IN BIN (WORKING SET) : 8590
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.99
REMARK 3 BIN R VALUE (WORKING SET) : 0.2670
REMARK 3 BIN FREE R VALUE SET COUNT : 428
REMARK 3 BIN FREE R VALUE : 0.2750
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 7042
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 154
REMARK 3 SOLVENT ATOMS : 889
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 23.60
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.41000
REMARK 3 B22 (A**2) : 1.88000
REMARK 3 B33 (A**2) : -1.47000
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): 0.091
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.088
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.066
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.941
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.967
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.959
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 7388 ; 0.009 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 7086 ; 0.002 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 9950 ; 1.490 ; 1.984
REMARK 3 BOND ANGLES OTHERS (DEGREES): 16485 ; 0.935 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 934 ; 5.731 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 289 ;33.434 ;25.571
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1319 ;12.969 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 12 ;16.417 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1151 ; 0.085 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 8110 ; 0.005 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 1406 ; 0.001 ; 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): 3727 ; 1.303 ; 2.140
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 3726 ; 1.303 ; 2.139
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 4664 ; 2.000 ; 3.203
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 4665 ; 2.000 ; 3.203
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 3661 ; 2.053 ; 2.450
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 3662 ; 2.053 ; 2.451
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 5287 ; 3.261 ; 3.562
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 8368 ; 4.887 ;27.128
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 8369 ; 4.887 ;27.133
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 NCS TYPE: LOCAL
REMARK 3 NUMBER OF DIFFERENT NCS PAIRS : 6
REMARK 3 GROUP CHAIN1 RANGE CHAIN2 RANGE COUNT RMS WEIGHT
REMARK 3 1 A 1 229 B 1 229 14798 0.05 0.05
REMARK 3 2 A 1 229 C 1 229 14572 0.06 0.05
REMARK 3 3 A -1 230 D -1 230 14806 0.05 0.05
REMARK 3 4 B 1 230 C 1 230 14882 0.06 0.05
REMARK 3 5 B 1 229 D 1 229 14912 0.06 0.05
REMARK 3 6 C 1 229 D 1 229 14886 0.05 0.05
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 : 1.20
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 6DYY COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 03-JUL-18.
REMARK 100 THE DEPOSITION ID IS D_1000235453.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 24-OCT-17
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 31-ID
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97931
REMARK 200 MONOCHROMATOR : DIAMOND(111)
REMARK 200 OPTICS : KB MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : RAYONIX MX225HE
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : IMOSFLM
REMARK 200 DATA SCALING SOFTWARE : AIMLESS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 123910
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.610
REMARK 200 RESOLUTION RANGE LOW (A) : 88.440
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 7.400
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 11.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.61
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.64
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 : 2.100
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 4WKP
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 44.31
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.20
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 200 MM CALCIUM CHLORIDE, 20% W/V
REMARK 280 PEG3350, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 295K
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 36.28200
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 88.44350
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 37.01400
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 88.44350
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 36.28200
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 37.01400
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
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: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 4270 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 17730 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -36.0 KCAL/MOL
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 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 4100 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 17590 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -22.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C
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 APPLY THE FOLLOWING TO CHAINS: D
REMARK 350 BIOMT1 2 1.000000 0.000000 0.000000 -36.28200
REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 185.07000
REMARK 350 BIOMT3 2 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 MET A -14
REMARK 465 GLY A -13
REMARK 465 HIS A -12
REMARK 465 HIS A -11
REMARK 465 HIS A -10
REMARK 465 HIS A -9
REMARK 465 HIS A -8
REMARK 465 HIS A -7
REMARK 465 GLU A -6
REMARK 465 ASN A -5
REMARK 465 LEU A -4
REMARK 465 TYR A -3
REMARK 465 PHE A -2
REMARK 465 MET B -14
REMARK 465 GLY B -13
REMARK 465 HIS B -12
REMARK 465 HIS B -11
REMARK 465 HIS B -10
REMARK 465 HIS B -9
REMARK 465 HIS B -8
REMARK 465 HIS B -7
REMARK 465 GLU B -6
REMARK 465 ASN B -5
REMARK 465 LEU B -4
REMARK 465 TYR B -3
REMARK 465 PHE B -2
REMARK 465 GLN B -1
REMARK 465 GLY B 0
REMARK 465 MET C -14
REMARK 465 GLY C -13
REMARK 465 HIS C -12
REMARK 465 HIS C -11
REMARK 465 HIS C -10
REMARK 465 HIS C -9
REMARK 465 HIS C -8
REMARK 465 HIS C -7
REMARK 465 GLU C -6
REMARK 465 ASN C -5
REMARK 465 LEU C -4
REMARK 465 TYR C -3
REMARK 465 PHE C -2
REMARK 465 GLN C -1
REMARK 465 GLY C 0
REMARK 465 MET D -14
REMARK 465 GLY D -13
REMARK 465 HIS D -12
REMARK 465 HIS D -11
REMARK 465 HIS D -10
REMARK 465 HIS D -9
REMARK 465 HIS D -8
REMARK 465 HIS D -7
REMARK 465 GLU D -6
REMARK 465 ASN D -5
REMARK 465 LEU D -4
REMARK 465 TYR D -3
REMARK 465 PHE D -2
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 LYS A 84 CD CE NZ
REMARK 470 LYS B 84 CD CE NZ
REMARK 470 LYS C 84 CD CE NZ
REMARK 470 GLN D -1 CG CD OE1 NE2
REMARK 470 LYS D 84 CD CE NZ
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 NZ LYS B 133 O HOH B 401 1.98
REMARK 500 NE2 GLN B 184 O HOH B 402 1.99
REMARK 500 NE2 GLN D 184 O HOH D 401 2.03
REMARK 500 OE2 GLU C 44 O HOH C 401 2.08
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 ND2 ASN B 42 ND2 ASN D 42 4465 1.95
REMARK 500
REMARK 500 REMARK: NULL
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 LEU A 193 CA - CB - CG ANGL. DEV. = 16.5 DEGREES
REMARK 500 ARG C 11 NE - CZ - NH2 ANGL. DEV. = -3.0 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 LYS A 51 162.80 83.95
REMARK 500 ASN A 89 -14.70 85.12
REMARK 500 SER A 117 -150.81 -137.13
REMARK 500 HIS A 155 46.06 -151.59
REMARK 500 GLU A 175 -24.59 -147.06
REMARK 500 ASP A 201 -167.57 -117.89
REMARK 500 LYS B 51 162.67 84.19
REMARK 500 ASN B 89 -14.57 85.06
REMARK 500 SER B 117 -150.89 -137.36
REMARK 500 HIS B 155 46.16 -152.01
REMARK 500 GLU B 175 -25.04 -146.66
REMARK 500 ASP B 201 -167.61 -118.41
REMARK 500 LYS C 51 161.96 84.39
REMARK 500 ASN C 89 -14.57 85.37
REMARK 500 SER C 117 -151.74 -138.24
REMARK 500 HIS C 155 46.48 -151.45
REMARK 500 GLU C 175 -24.72 -146.18
REMARK 500 ASP C 201 -167.80 -117.72
REMARK 500 LYS D 51 161.98 84.14
REMARK 500 ASN D 89 -14.16 84.88
REMARK 500 SER D 117 -151.82 -137.67
REMARK 500 HIS D 155 46.29 -151.06
REMARK 500 GLU D 175 -24.57 -146.19
REMARK 500 ASP D 201 -167.79 -117.68
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 MG A 302 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH A 401 O
REMARK 620 2 HOH A 403 O 100.7
REMARK 620 3 HOH A 418 O 85.3 86.3
REMARK 620 4 HOH A 428 O 92.3 85.9 171.3
REMARK 620 5 HOH A 579 O 88.7 170.2 97.2 91.1
REMARK 620 6 HOH A 591 O 177.2 80.1 97.4 85.1 90.3
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG B 304 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH B 401 O
REMARK 620 2 HOH B 411 O 87.5
REMARK 620 3 HOH B 424 O 92.1 81.4
REMARK 620 4 HOH B 453 O 87.7 168.1 88.0
REMARK 620 5 HOH B 585 O 83.4 98.7 175.5 91.5
REMARK 620 6 HOH B 601 O 168.5 94.5 99.4 92.3 85.1
REMARK 620 N 1 2 3 4 5
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue OS6 A 303
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 303
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG B 304
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue OS6 B 305
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO C 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO C 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue OS6 C 303
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO D 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue OS6 D 302
DBREF1 6DYY A 1 230 UNP A0A1W0VQJ9_HELPX
DBREF2 6DYY A A0A1W0VQJ9 2 231
DBREF1 6DYY B 1 230 UNP A0A1W0VQJ9_HELPX
DBREF2 6DYY B A0A1W0VQJ9 2 231
DBREF1 6DYY C 1 230 UNP A0A1W0VQJ9_HELPX
DBREF2 6DYY C A0A1W0VQJ9 2 231
DBREF1 6DYY D 1 230 UNP A0A1W0VQJ9_HELPX
DBREF2 6DYY D A0A1W0VQJ9 2 231
SEQADV 6DYY MET A -14 UNP A0A1W0VQJ EXPRESSION TAG
SEQADV 6DYY GLY A -13 UNP A0A1W0VQJ EXPRESSION TAG
SEQADV 6DYY HIS A -12 UNP A0A1W0VQJ EXPRESSION TAG
SEQADV 6DYY HIS A -11 UNP A0A1W0VQJ EXPRESSION TAG
SEQADV 6DYY HIS A -10 UNP A0A1W0VQJ EXPRESSION TAG
SEQADV 6DYY HIS A -9 UNP A0A1W0VQJ EXPRESSION TAG
SEQADV 6DYY HIS A -8 UNP A0A1W0VQJ EXPRESSION TAG
SEQADV 6DYY HIS A -7 UNP A0A1W0VQJ EXPRESSION TAG
SEQADV 6DYY GLU A -6 UNP A0A1W0VQJ EXPRESSION TAG
SEQADV 6DYY ASN A -5 UNP A0A1W0VQJ EXPRESSION TAG
SEQADV 6DYY LEU A -4 UNP A0A1W0VQJ EXPRESSION TAG
SEQADV 6DYY TYR A -3 UNP A0A1W0VQJ EXPRESSION TAG
SEQADV 6DYY PHE A -2 UNP A0A1W0VQJ EXPRESSION TAG
SEQADV 6DYY GLN A -1 UNP A0A1W0VQJ EXPRESSION TAG
SEQADV 6DYY GLY A 0 UNP A0A1W0VQJ EXPRESSION TAG
SEQADV 6DYY MET B -14 UNP A0A1W0VQJ EXPRESSION TAG
SEQADV 6DYY GLY B -13 UNP A0A1W0VQJ EXPRESSION TAG
SEQADV 6DYY HIS B -12 UNP A0A1W0VQJ EXPRESSION TAG
SEQADV 6DYY HIS B -11 UNP A0A1W0VQJ EXPRESSION TAG
SEQADV 6DYY HIS B -10 UNP A0A1W0VQJ EXPRESSION TAG
SEQADV 6DYY HIS B -9 UNP A0A1W0VQJ EXPRESSION TAG
SEQADV 6DYY HIS B -8 UNP A0A1W0VQJ EXPRESSION TAG
SEQADV 6DYY HIS B -7 UNP A0A1W0VQJ EXPRESSION TAG
SEQADV 6DYY GLU B -6 UNP A0A1W0VQJ EXPRESSION TAG
SEQADV 6DYY ASN B -5 UNP A0A1W0VQJ EXPRESSION TAG
SEQADV 6DYY LEU B -4 UNP A0A1W0VQJ EXPRESSION TAG
SEQADV 6DYY TYR B -3 UNP A0A1W0VQJ EXPRESSION TAG
SEQADV 6DYY PHE B -2 UNP A0A1W0VQJ EXPRESSION TAG
SEQADV 6DYY GLN B -1 UNP A0A1W0VQJ EXPRESSION TAG
SEQADV 6DYY GLY B 0 UNP A0A1W0VQJ EXPRESSION TAG
SEQADV 6DYY MET C -14 UNP A0A1W0VQJ EXPRESSION TAG
SEQADV 6DYY GLY C -13 UNP A0A1W0VQJ EXPRESSION TAG
SEQADV 6DYY HIS C -12 UNP A0A1W0VQJ EXPRESSION TAG
SEQADV 6DYY HIS C -11 UNP A0A1W0VQJ EXPRESSION TAG
SEQADV 6DYY HIS C -10 UNP A0A1W0VQJ EXPRESSION TAG
SEQADV 6DYY HIS C -9 UNP A0A1W0VQJ EXPRESSION TAG
SEQADV 6DYY HIS C -8 UNP A0A1W0VQJ EXPRESSION TAG
SEQADV 6DYY HIS C -7 UNP A0A1W0VQJ EXPRESSION TAG
SEQADV 6DYY GLU C -6 UNP A0A1W0VQJ EXPRESSION TAG
SEQADV 6DYY ASN C -5 UNP A0A1W0VQJ EXPRESSION TAG
SEQADV 6DYY LEU C -4 UNP A0A1W0VQJ EXPRESSION TAG
SEQADV 6DYY TYR C -3 UNP A0A1W0VQJ EXPRESSION TAG
SEQADV 6DYY PHE C -2 UNP A0A1W0VQJ EXPRESSION TAG
SEQADV 6DYY GLN C -1 UNP A0A1W0VQJ EXPRESSION TAG
SEQADV 6DYY GLY C 0 UNP A0A1W0VQJ EXPRESSION TAG
SEQADV 6DYY MET D -14 UNP A0A1W0VQJ EXPRESSION TAG
SEQADV 6DYY GLY D -13 UNP A0A1W0VQJ EXPRESSION TAG
SEQADV 6DYY HIS D -12 UNP A0A1W0VQJ EXPRESSION TAG
SEQADV 6DYY HIS D -11 UNP A0A1W0VQJ EXPRESSION TAG
SEQADV 6DYY HIS D -10 UNP A0A1W0VQJ EXPRESSION TAG
SEQADV 6DYY HIS D -9 UNP A0A1W0VQJ EXPRESSION TAG
SEQADV 6DYY HIS D -8 UNP A0A1W0VQJ EXPRESSION TAG
SEQADV 6DYY HIS D -7 UNP A0A1W0VQJ EXPRESSION TAG
SEQADV 6DYY GLU D -6 UNP A0A1W0VQJ EXPRESSION TAG
SEQADV 6DYY ASN D -5 UNP A0A1W0VQJ EXPRESSION TAG
SEQADV 6DYY LEU D -4 UNP A0A1W0VQJ EXPRESSION TAG
SEQADV 6DYY TYR D -3 UNP A0A1W0VQJ EXPRESSION TAG
SEQADV 6DYY PHE D -2 UNP A0A1W0VQJ EXPRESSION TAG
SEQADV 6DYY GLN D -1 UNP A0A1W0VQJ EXPRESSION TAG
SEQADV 6DYY GLY D 0 UNP A0A1W0VQJ EXPRESSION TAG
SEQRES 1 A 245 MET GLY HIS HIS HIS HIS HIS HIS GLU ASN LEU TYR PHE
SEQRES 2 A 245 GLN GLY VAL GLN LYS ILE GLY ILE LEU GLY ALA MET ARG
SEQRES 3 A 245 GLU GLU ILE THR PRO ILE LEU GLU LEU PHE GLY VAL ASP
SEQRES 4 A 245 PHE GLU GLU ILE PRO LEU GLY GLY ASN VAL PHE HIS LYS
SEQRES 5 A 245 GLY VAL TYR HIS ASN LYS GLU ILE ILE VAL ALA TYR SER
SEQRES 6 A 245 LYS ILE GLY LYS VAL HIS SER THR LEU THR THR THR SER
SEQRES 7 A 245 MET ILE LEU ALA PHE GLY VAL GLN LYS VAL LEU PHE SER
SEQRES 8 A 245 GLY VAL ALA GLY SER LEU VAL LYS ASP LEU LYS ILE ASN
SEQRES 9 A 245 ASP LEU LEU VAL ALA THR GLN LEU VAL GLN HIS ASP VAL
SEQRES 10 A 245 ASP LEU SER ALA PHE ASP HIS PRO LEU GLY PHE ILE PRO
SEQRES 11 A 245 GLU SER ALA ILE PHE ILE GLU THR SER GLY SER LEU ASN
SEQRES 12 A 245 ALA LEU ALA LYS LYS ILE ALA ASN GLU GLN HIS ILE ALA
SEQRES 13 A 245 LEU LYS GLU GLY VAL ILE ALA SER GLY ASP GLN PHE VAL
SEQRES 14 A 245 HIS SER LYS GLU ARG LYS GLU PHE LEU VAL SER GLU PHE
SEQRES 15 A 245 LYS ALA SER ALA VAL GLU MET GLU GLY ALA SER VAL ALA
SEQRES 16 A 245 PHE VAL CYS GLN LYS PHE GLY VAL PRO CYS CYS VAL LEU
SEQRES 17 A 245 ARG SER ILE SER ASP ASN ALA ASP GLU LYS ALA GLY MET
SEQRES 18 A 245 SER PHE ASP GLU PHE LEU GLU LYS SER ALA HIS THR SER
SEQRES 19 A 245 ALA LYS PHE LEU LYS SER MET VAL ASP GLU LEU
SEQRES 1 B 245 MET GLY HIS HIS HIS HIS HIS HIS GLU ASN LEU TYR PHE
SEQRES 2 B 245 GLN GLY VAL GLN LYS ILE GLY ILE LEU GLY ALA MET ARG
SEQRES 3 B 245 GLU GLU ILE THR PRO ILE LEU GLU LEU PHE GLY VAL ASP
SEQRES 4 B 245 PHE GLU GLU ILE PRO LEU GLY GLY ASN VAL PHE HIS LYS
SEQRES 5 B 245 GLY VAL TYR HIS ASN LYS GLU ILE ILE VAL ALA TYR SER
SEQRES 6 B 245 LYS ILE GLY LYS VAL HIS SER THR LEU THR THR THR SER
SEQRES 7 B 245 MET ILE LEU ALA PHE GLY VAL GLN LYS VAL LEU PHE SER
SEQRES 8 B 245 GLY VAL ALA GLY SER LEU VAL LYS ASP LEU LYS ILE ASN
SEQRES 9 B 245 ASP LEU LEU VAL ALA THR GLN LEU VAL GLN HIS ASP VAL
SEQRES 10 B 245 ASP LEU SER ALA PHE ASP HIS PRO LEU GLY PHE ILE PRO
SEQRES 11 B 245 GLU SER ALA ILE PHE ILE GLU THR SER GLY SER LEU ASN
SEQRES 12 B 245 ALA LEU ALA LYS LYS ILE ALA ASN GLU GLN HIS ILE ALA
SEQRES 13 B 245 LEU LYS GLU GLY VAL ILE ALA SER GLY ASP GLN PHE VAL
SEQRES 14 B 245 HIS SER LYS GLU ARG LYS GLU PHE LEU VAL SER GLU PHE
SEQRES 15 B 245 LYS ALA SER ALA VAL GLU MET GLU GLY ALA SER VAL ALA
SEQRES 16 B 245 PHE VAL CYS GLN LYS PHE GLY VAL PRO CYS CYS VAL LEU
SEQRES 17 B 245 ARG SER ILE SER ASP ASN ALA ASP GLU LYS ALA GLY MET
SEQRES 18 B 245 SER PHE ASP GLU PHE LEU GLU LYS SER ALA HIS THR SER
SEQRES 19 B 245 ALA LYS PHE LEU LYS SER MET VAL ASP GLU LEU
SEQRES 1 C 245 MET GLY HIS HIS HIS HIS HIS HIS GLU ASN LEU TYR PHE
SEQRES 2 C 245 GLN GLY VAL GLN LYS ILE GLY ILE LEU GLY ALA MET ARG
SEQRES 3 C 245 GLU GLU ILE THR PRO ILE LEU GLU LEU PHE GLY VAL ASP
SEQRES 4 C 245 PHE GLU GLU ILE PRO LEU GLY GLY ASN VAL PHE HIS LYS
SEQRES 5 C 245 GLY VAL TYR HIS ASN LYS GLU ILE ILE VAL ALA TYR SER
SEQRES 6 C 245 LYS ILE GLY LYS VAL HIS SER THR LEU THR THR THR SER
SEQRES 7 C 245 MET ILE LEU ALA PHE GLY VAL GLN LYS VAL LEU PHE SER
SEQRES 8 C 245 GLY VAL ALA GLY SER LEU VAL LYS ASP LEU LYS ILE ASN
SEQRES 9 C 245 ASP LEU LEU VAL ALA THR GLN LEU VAL GLN HIS ASP VAL
SEQRES 10 C 245 ASP LEU SER ALA PHE ASP HIS PRO LEU GLY PHE ILE PRO
SEQRES 11 C 245 GLU SER ALA ILE PHE ILE GLU THR SER GLY SER LEU ASN
SEQRES 12 C 245 ALA LEU ALA LYS LYS ILE ALA ASN GLU GLN HIS ILE ALA
SEQRES 13 C 245 LEU LYS GLU GLY VAL ILE ALA SER GLY ASP GLN PHE VAL
SEQRES 14 C 245 HIS SER LYS GLU ARG LYS GLU PHE LEU VAL SER GLU PHE
SEQRES 15 C 245 LYS ALA SER ALA VAL GLU MET GLU GLY ALA SER VAL ALA
SEQRES 16 C 245 PHE VAL CYS GLN LYS PHE GLY VAL PRO CYS CYS VAL LEU
SEQRES 17 C 245 ARG SER ILE SER ASP ASN ALA ASP GLU LYS ALA GLY MET
SEQRES 18 C 245 SER PHE ASP GLU PHE LEU GLU LYS SER ALA HIS THR SER
SEQRES 19 C 245 ALA LYS PHE LEU LYS SER MET VAL ASP GLU LEU
SEQRES 1 D 245 MET GLY HIS HIS HIS HIS HIS HIS GLU ASN LEU TYR PHE
SEQRES 2 D 245 GLN GLY VAL GLN LYS ILE GLY ILE LEU GLY ALA MET ARG
SEQRES 3 D 245 GLU GLU ILE THR PRO ILE LEU GLU LEU PHE GLY VAL ASP
SEQRES 4 D 245 PHE GLU GLU ILE PRO LEU GLY GLY ASN VAL PHE HIS LYS
SEQRES 5 D 245 GLY VAL TYR HIS ASN LYS GLU ILE ILE VAL ALA TYR SER
SEQRES 6 D 245 LYS ILE GLY LYS VAL HIS SER THR LEU THR THR THR SER
SEQRES 7 D 245 MET ILE LEU ALA PHE GLY VAL GLN LYS VAL LEU PHE SER
SEQRES 8 D 245 GLY VAL ALA GLY SER LEU VAL LYS ASP LEU LYS ILE ASN
SEQRES 9 D 245 ASP LEU LEU VAL ALA THR GLN LEU VAL GLN HIS ASP VAL
SEQRES 10 D 245 ASP LEU SER ALA PHE ASP HIS PRO LEU GLY PHE ILE PRO
SEQRES 11 D 245 GLU SER ALA ILE PHE ILE GLU THR SER GLY SER LEU ASN
SEQRES 12 D 245 ALA LEU ALA LYS LYS ILE ALA ASN GLU GLN HIS ILE ALA
SEQRES 13 D 245 LEU LYS GLU GLY VAL ILE ALA SER GLY ASP GLN PHE VAL
SEQRES 14 D 245 HIS SER LYS GLU ARG LYS GLU PHE LEU VAL SER GLU PHE
SEQRES 15 D 245 LYS ALA SER ALA VAL GLU MET GLU GLY ALA SER VAL ALA
SEQRES 16 D 245 PHE VAL CYS GLN LYS PHE GLY VAL PRO CYS CYS VAL LEU
SEQRES 17 D 245 ARG SER ILE SER ASP ASN ALA ASP GLU LYS ALA GLY MET
SEQRES 18 D 245 SER PHE ASP GLU PHE LEU GLU LYS SER ALA HIS THR SER
SEQRES 19 D 245 ALA LYS PHE LEU LYS SER MET VAL ASP GLU LEU
HET EDO A 301 4
HET MG A 302 1
HET OS6 A 303 31
HET EDO B 301 4
HET EDO B 302 4
HET EDO B 303 4
HET MG B 304 1
HET OS6 B 305 31
HET EDO C 301 4
HET EDO C 302 4
HET OS6 C 303 31
HET EDO D 301 4
HET OS6 D 302 31
HETNAM EDO 1,2-ETHANEDIOL
HETNAM MG MAGNESIUM ION
HETNAM OS6 (3R,4S)-1-[(4-AMINO-5H-PYRROLO[3,2-D]PYRIMIDIN-7-YL)
HETNAM 2 OS6 METHYL]-4-({[3-(1-BUTYL-1H-1,2,3-TRIAZOL-4-YL)
HETNAM 3 OS6 PROPYL]SULFANYL}METHYL)PYRROLIDIN-3-OL
HETSYN EDO ETHYLENE GLYCOL
FORMUL 5 EDO 7(C2 H6 O2)
FORMUL 6 MG 2(MG 2+)
FORMUL 7 OS6 4(C21 H32 N8 O S)
FORMUL 18 HOH *889(H2 O)
HELIX 1 AA1 MET A 10 GLY A 22 1 13
HELIX 2 AA2 GLY A 53 GLY A 69 1 17
HELIX 3 AA3 LEU A 104 ASP A 108 5 5
HELIX 4 AA4 SER A 124 HIS A 139 1 16
HELIX 5 AA5 SER A 156 LYS A 168 1 13
HELIX 6 AA6 GLU A 175 GLY A 187 1 13
HELIX 7 AA7 LYS A 203 ASP A 228 1 26
HELIX 8 AA8 MET B 10 GLY B 22 1 13
HELIX 9 AA9 GLY B 53 GLY B 69 1 17
HELIX 10 AB1 LEU B 104 ASP B 108 5 5
HELIX 11 AB2 SER B 124 HIS B 139 1 16
HELIX 12 AB3 SER B 156 LYS B 168 1 13
HELIX 13 AB4 GLU B 175 GLY B 187 1 13
HELIX 14 AB5 LYS B 203 ASP B 228 1 26
HELIX 15 AB6 MET C 10 GLY C 22 1 13
HELIX 16 AB7 GLY C 53 GLY C 69 1 17
HELIX 17 AB8 LEU C 104 ASP C 108 5 5
HELIX 18 AB9 SER C 124 HIS C 139 1 16
HELIX 19 AC1 SER C 156 LYS C 168 1 13
HELIX 20 AC2 GLU C 175 GLY C 187 1 13
HELIX 21 AC3 LYS C 203 LEU C 230 1 28
HELIX 22 AC4 MET D 10 GLY D 22 1 13
HELIX 23 AC5 GLY D 53 GLY D 69 1 17
HELIX 24 AC6 LEU D 104 ASP D 108 5 5
HELIX 25 AC7 SER D 124 HIS D 139 1 16
HELIX 26 AC8 SER D 156 LYS D 168 1 13
HELIX 27 AC9 GLU D 175 GLY D 187 1 13
HELIX 28 AD1 LYS D 203 GLU D 229 1 27
SHEET 1 AA1 9 GLU A 26 LEU A 30 0
SHEET 2 AA1 9 ASN A 33 TYR A 40 -1 O PHE A 35 N ILE A 28
SHEET 3 AA1 9 LYS A 43 TYR A 49 -1 O VAL A 47 N HIS A 36
SHEET 4 AA1 9 GLN A 2 GLY A 8 1 N ILE A 6 O ILE A 46
SHEET 5 AA1 9 LYS A 72 SER A 81 1 O LYS A 72 N GLY A 5
SHEET 6 AA1 9 ALA A 169 GLU A 173 -1 O VAL A 172 N GLY A 80
SHEET 7 AA1 9 LEU A 142 SER A 149 1 N VAL A 146 O SER A 170
SHEET 8 AA1 9 LEU A 91 GLN A 99 1 N VAL A 98 O SER A 149
SHEET 9 AA1 9 ILE A 121 GLU A 122 -1 O ILE A 121 N LEU A 97
SHEET 1 AA2 8 GLU A 26 LEU A 30 0
SHEET 2 AA2 8 ASN A 33 TYR A 40 -1 O PHE A 35 N ILE A 28
SHEET 3 AA2 8 LYS A 43 TYR A 49 -1 O VAL A 47 N HIS A 36
SHEET 4 AA2 8 GLN A 2 GLY A 8 1 N ILE A 6 O ILE A 46
SHEET 5 AA2 8 LYS A 72 SER A 81 1 O LYS A 72 N GLY A 5
SHEET 6 AA2 8 CYS A 190 ASP A 198 1 O ASP A 198 N SER A 81
SHEET 7 AA2 8 LEU A 91 GLN A 99 -1 N LEU A 92 O ARG A 194
SHEET 8 AA2 8 ILE A 121 GLU A 122 -1 O ILE A 121 N LEU A 97
SHEET 1 AA3 9 GLU B 26 LEU B 30 0
SHEET 2 AA3 9 ASN B 33 TYR B 40 -1 O PHE B 35 N ILE B 28
SHEET 3 AA3 9 LYS B 43 TYR B 49 -1 O VAL B 47 N HIS B 36
SHEET 4 AA3 9 GLN B 2 GLY B 8 1 N ILE B 6 O ILE B 46
SHEET 5 AA3 9 LYS B 72 SER B 81 1 O LYS B 72 N GLY B 5
SHEET 6 AA3 9 ALA B 169 GLU B 173 -1 O VAL B 172 N GLY B 80
SHEET 7 AA3 9 LEU B 142 SER B 149 1 N VAL B 146 O SER B 170
SHEET 8 AA3 9 LEU B 91 GLN B 99 1 N VAL B 98 O SER B 149
SHEET 9 AA3 9 ILE B 121 GLU B 122 -1 O ILE B 121 N LEU B 97
SHEET 1 AA4 8 GLU B 26 LEU B 30 0
SHEET 2 AA4 8 ASN B 33 TYR B 40 -1 O PHE B 35 N ILE B 28
SHEET 3 AA4 8 LYS B 43 TYR B 49 -1 O VAL B 47 N HIS B 36
SHEET 4 AA4 8 GLN B 2 GLY B 8 1 N ILE B 6 O ILE B 46
SHEET 5 AA4 8 LYS B 72 SER B 81 1 O LYS B 72 N GLY B 5
SHEET 6 AA4 8 CYS B 190 ASP B 198 1 O ASP B 198 N SER B 81
SHEET 7 AA4 8 LEU B 91 GLN B 99 -1 N LEU B 92 O ARG B 194
SHEET 8 AA4 8 ILE B 121 GLU B 122 -1 O ILE B 121 N LEU B 97
SHEET 1 AA5 9 GLU C 26 LEU C 30 0
SHEET 2 AA5 9 ASN C 33 TYR C 40 -1 O PHE C 35 N ILE C 28
SHEET 3 AA5 9 LYS C 43 TYR C 49 -1 O VAL C 47 N HIS C 36
SHEET 4 AA5 9 GLN C 2 GLY C 8 1 N ILE C 6 O ILE C 46
SHEET 5 AA5 9 LYS C 72 SER C 81 1 O LYS C 72 N GLY C 5
SHEET 6 AA5 9 ALA C 169 GLU C 173 -1 O VAL C 172 N GLY C 80
SHEET 7 AA5 9 LEU C 142 SER C 149 1 N VAL C 146 O SER C 170
SHEET 8 AA5 9 LEU C 91 GLN C 99 1 N VAL C 98 O SER C 149
SHEET 9 AA5 9 ILE C 121 GLU C 122 -1 O ILE C 121 N LEU C 97
SHEET 1 AA6 8 GLU C 26 LEU C 30 0
SHEET 2 AA6 8 ASN C 33 TYR C 40 -1 O PHE C 35 N ILE C 28
SHEET 3 AA6 8 LYS C 43 TYR C 49 -1 O VAL C 47 N HIS C 36
SHEET 4 AA6 8 GLN C 2 GLY C 8 1 N ILE C 6 O ILE C 46
SHEET 5 AA6 8 LYS C 72 SER C 81 1 O LYS C 72 N GLY C 5
SHEET 6 AA6 8 CYS C 190 ASP C 198 1 O ASP C 198 N SER C 81
SHEET 7 AA6 8 LEU C 91 GLN C 99 -1 N LEU C 92 O ARG C 194
SHEET 8 AA6 8 ILE C 121 GLU C 122 -1 O ILE C 121 N LEU C 97
SHEET 1 AA7 9 GLU D 26 LEU D 30 0
SHEET 2 AA7 9 ASN D 33 TYR D 40 -1 O PHE D 35 N ILE D 28
SHEET 3 AA7 9 LYS D 43 TYR D 49 -1 O VAL D 47 N HIS D 36
SHEET 4 AA7 9 GLN D 2 GLY D 8 1 N ILE D 4 O GLU D 44
SHEET 5 AA7 9 LYS D 72 SER D 81 1 O LYS D 72 N GLY D 5
SHEET 6 AA7 9 ALA D 169 GLU D 173 -1 O VAL D 172 N GLY D 80
SHEET 7 AA7 9 LEU D 142 SER D 149 1 N VAL D 146 O SER D 170
SHEET 8 AA7 9 LEU D 91 GLN D 99 1 N VAL D 98 O SER D 149
SHEET 9 AA7 9 ILE D 121 GLU D 122 -1 O ILE D 121 N LEU D 97
SHEET 1 AA8 8 GLU D 26 LEU D 30 0
SHEET 2 AA8 8 ASN D 33 TYR D 40 -1 O PHE D 35 N ILE D 28
SHEET 3 AA8 8 LYS D 43 TYR D 49 -1 O VAL D 47 N HIS D 36
SHEET 4 AA8 8 GLN D 2 GLY D 8 1 N ILE D 4 O GLU D 44
SHEET 5 AA8 8 LYS D 72 SER D 81 1 O LYS D 72 N GLY D 5
SHEET 6 AA8 8 CYS D 190 ASP D 198 1 O ASP D 198 N SER D 81
SHEET 7 AA8 8 LEU D 91 GLN D 99 -1 N LEU D 92 O ARG D 194
SHEET 8 AA8 8 ILE D 121 GLU D 122 -1 O ILE D 121 N LEU D 97
LINK MG MG A 302 O HOH A 401 1555 3655 2.03
LINK MG MG A 302 O HOH A 403 1555 3655 2.17
LINK MG MG A 302 O HOH A 418 1555 1555 1.99
LINK MG MG A 302 O HOH A 428 1555 3655 2.08
LINK MG MG A 302 O HOH A 579 1555 3655 2.16
LINK MG MG A 302 O HOH A 591 1555 1555 2.04
LINK MG MG B 304 O HOH B 401 1555 1555 1.94
LINK MG MG B 304 O HOH B 411 1555 4475 1.99
LINK MG MG B 304 O HOH B 424 1555 1555 2.21
LINK MG MG B 304 O HOH B 453 1555 1555 2.01
LINK MG MG B 304 O HOH B 585 1555 4475 2.00
LINK MG MG B 304 O HOH B 601 1555 1555 1.98
SITE 1 AC1 6 THR A 123 GLY A 125 SER A 126 HOH A 464
SITE 2 AC1 6 ASP C 209 PHE D 107
SITE 1 AC2 7 GLU A 229 HOH A 401 HOH A 403 HOH A 418
SITE 2 AC2 7 HOH A 428 HOH A 579 HOH A 591
SITE 1 AC3 19 ILE A 52 VAL A 78 ALA A 79 GLY A 80
SITE 2 AC3 19 GLN A 152 PHE A 153 VAL A 154 VAL A 172
SITE 3 AC3 19 GLU A 173 MET A 174 GLU A 175 SER A 197
SITE 4 AC3 19 ASP A 198 ALA A 200 PHE A 208 HOH A 416
SITE 5 AC3 19 HIS B 109 PRO B 115 GLU B 116
SITE 1 AC4 7 THR B 123 GLY B 125 SER B 126 HOH B 403
SITE 2 AC4 7 HOH B 562 PHE C 107 ASP D 209
SITE 1 AC5 7 ALA A 106 PHE A 107 GLY B 205 MET B 206
SITE 2 AC5 7 ASP B 209 HOH B 457 HOH B 492
SITE 1 AC6 6 GLN B 138 HIS B 139 SER B 165 GLU B 166
SITE 2 AC6 6 HOH B 536 HOH B 546
SITE 1 AC7 7 LYS B 133 HOH B 401 HOH B 411 HOH B 424
SITE 2 AC7 7 HOH B 453 HOH B 585 HOH B 601
SITE 1 AC8 21 LEU A 104 HIS A 109 PRO A 115 ALA B 9
SITE 2 AC8 21 ILE B 52 VAL B 78 ALA B 79 GLY B 80
SITE 3 AC8 21 GLN B 152 PHE B 153 VAL B 154 VAL B 172
SITE 4 AC8 21 GLU B 173 MET B 174 GLU B 175 SER B 197
SITE 5 AC8 21 ASP B 198 PHE B 208 HOH B 423 LYS C 132
SITE 6 AC8 21 HOH C 483
SITE 1 AC9 5 GLY C 32 ASN C 33 VAL C 34 TYR C 49
SITE 2 AC9 5 HOH C 478
SITE 1 AD1 6 LYS A 157 SER C 156 LYS C 157 ASP C 201
SITE 2 AD1 6 GLU C 202 HOH C 413
SITE 1 AD2 19 GLU A 122 ALA C 9 ILE C 52 VAL C 78
SITE 2 AD2 19 ALA C 79 GLY C 80 GLN C 152 PHE C 153
SITE 3 AD2 19 VAL C 154 VAL C 172 GLU C 173 MET C 174
SITE 4 AD2 19 GLU C 175 SER C 197 ASP C 198 PHE C 208
SITE 5 AD2 19 HOH C 417 PHE D 107 HIS D 109
SITE 1 AD3 5 GLY D 32 ASN D 33 VAL D 34 TYR D 49
SITE 2 AD3 5 HOH D 446
SITE 1 AD4 16 HIS C 109 ALA D 9 ILE D 52 VAL D 78
SITE 2 AD4 16 ALA D 79 GLY D 80 PHE D 153 VAL D 154
SITE 3 AD4 16 VAL D 172 GLU D 173 MET D 174 GLU D 175
SITE 4 AD4 16 SER D 197 ASP D 198 PHE D 208 HOH D 410
CRYST1 72.564 74.028 176.887 90.00 90.00 90.00 P 21 21 21 16
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 0.013781 0.000000 0.000000 0.00000
SCALE2 0.000000 0.013508 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005653 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
