HEADER LYASE 29-MAR-10 3MCI
TITLE CRYSTAL STRUCTURE OF MOLYBDENUM COFACTOR BIOSYNTHESIS (AQ_061) FROM
TITLE 2 AQUIFEX AEOLICUS VF5
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: MOLYBDENUM COFACTOR BIOSYNTHESIS MOG;
COMPND 3 CHAIN: A, B, C;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: AQUIFEX AEOLICUS;
SOURCE 3 ORGANISM_TAXID: 224324;
SOURCE 4 STRAIN: VF5;
SOURCE 5 GENE: MOG, AQ_061;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL-21 CONDON PLUS (DE3)-RIL;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET21A
KEYWDS MOLYBDOPTERIN, MPT, STRUCTURAL GENOMICS, NPPSFA, NATIONAL PROJECT ON
KEYWDS 2 PROTEIN STRUCTURAL AND FUNCTIONAL ANALYSES, RIKEN STRUCTURAL
KEYWDS 3 GENOMICS/PROTEOMICS INITIATIVE, RSGI, LYASE
EXPDTA X-RAY DIFFRACTION
AUTHOR J.JEYAKANTHAN,S.P.KANAUJIA,K.SEKAR,Y.AGARI,A.EBIHARA,S.KURAMITSU,
AUTHOR 2 A.SHINKAI,Y.SHIRO,S.YOKOYAMA,RIKEN STRUCTURAL GENOMICS/PROTEOMICS
AUTHOR 3 INITIATIVE (RSGI)
REVDAT 2 01-NOV-23 3MCI 1 REMARK
REVDAT 1 19-JAN-11 3MCI 0
JRNL AUTH S.P.KANAUJIA,J.JEYAKANTHAN,A.SHINKAI,S.KURAMITSU,S.YOKOYAMA,
JRNL AUTH 2 K.SEKAR
JRNL TITL CRYSTAL STRUCTURES, DYNAMICS AND FUNCTIONAL IMPLICATIONS OF
JRNL TITL 2 MOLYBDENUM-COFACTOR BIOSYNTHESIS PROTEIN MOGA FROM TWO
JRNL TITL 3 THERMOPHILIC ORGANISMS
JRNL REF ACTA CRYSTALLOGR.,SECT.F V. 67 2 2011
JRNL REFN ESSN 1744-3091
JRNL PMID 21206014
JRNL DOI 10.1107/S1744309110035037
REMARK 2
REMARK 2 RESOLUTION. 1.70 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.2
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.70
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 39.76
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 217492.010
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 96.7
REMARK 3 NUMBER OF REFLECTIONS : 51884
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 SET) : 0.195
REMARK 3 FREE R VALUE : 0.227
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 2605
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.004
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 6
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.70
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.81
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 88.20
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 7482
REMARK 3 BIN R VALUE (WORKING SET) : 0.2670
REMARK 3 BIN FREE R VALUE : 0.2870
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5.30
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 418
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.014
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3987
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 38
REMARK 3 SOLVENT ATOMS : 625
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 20.40
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 26.80
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 4.32000
REMARK 3 B22 (A**2) : 2.06000
REMARK 3 B33 (A**2) : -6.38000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -1.28000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.20
REMARK 3 ESD FROM SIGMAA (A) : 0.16
REMARK 3 LOW RESOLUTION CUTOFF (A) : 5.00
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.24
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.19
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.006
REMARK 3 BOND ANGLES (DEGREES) : 1.300
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 23.00
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.970
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : RESTRAINED
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.35
REMARK 3 BSOL : 54.73
REMARK 3
REMARK 3 NCS MODEL : NULL
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : PROTEIN_REP.PARAM
REMARK 3 PARAMETER FILE 2 : WATER_REP.PARAM
REMARK 3 PARAMETER FILE 3 : ION.PARAM
REMARK 3 PARAMETER FILE 4 : LIGAND.PARAM
REMARK 3 PARAMETER FILE 5 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : ION.TOP
REMARK 3 TOPOLOGY FILE 3 : WATER_PROTIN.TOP
REMARK 3 TOPOLOGY FILE 4 : LIGAND.TOP
REMARK 3 TOPOLOGY FILE 5 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 3MCI COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 13-APR-10.
REMARK 100 THE DEPOSITION ID IS D_1000058378.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 18-DEC-06
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 9.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SPRING-8
REMARK 200 BEAMLINE : BL26B2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0
REMARK 200 MONOCHROMATOR : SI 1 1 1 DOUBLE CRYSTAL
REMARK 200 MONOCHROMATOR
REMARK 200 OPTICS : RH COATED BENT-CYRINDRICAL,
REMARK 200 MIRROR
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : RIGAKU JUPITER 210
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 53022
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.700
REMARK 200 RESOLUTION RANGE LOW (A) : 40.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : 0.05400
REMARK 200 R SYM (I) : 0.05000
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) : 1.70
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.76
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.9
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.26700
REMARK 200 R SYM FOR SHELL (I) : 0.23000
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: 2FUW
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 42.85
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.15
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 40% PEG 600, 100MM CES, PH 9.5, VAPOR
REMARK 280 DIFFUSION, SITTING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 56.57950
REMARK 290 SMTRY3 2 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: TRIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 4400 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 22040 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -34.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, 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 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 1
REMARK 465 MET B 1
REMARK 465 SER B 2
REMARK 465 LYS B 178
REMARK 465 MET C 1
REMARK 465 SER C 2
REMARK 465 LYS C 178
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 179
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 180
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG A 181
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG A 182
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO C 179
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO C 180
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO C 182
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2PBQ RELATED DB: PDB
REMARK 900 RELATED ID: 3MCJ RELATED DB: PDB
DBREF 3MCI A 1 178 UNP O66472 O66472_AQUAE 1 178
DBREF 3MCI B 1 178 UNP O66472 O66472_AQUAE 1 178
DBREF 3MCI C 1 178 UNP O66472 O66472_AQUAE 1 178
SEQRES 1 A 178 MET SER GLU LYS LYS ALA VAL ILE GLY VAL VAL THR ILE
SEQRES 2 A 178 SER ASP ARG ALA SER LYS GLY ILE TYR GLU ASP ILE SER
SEQRES 3 A 178 GLY LYS ALA ILE ILE ASP TYR LEU LYS ASP VAL ILE ILE
SEQRES 4 A 178 THR PRO PHE GLU VAL GLU TYR ARG VAL ILE PRO ASP GLU
SEQRES 5 A 178 ARG ASP LEU ILE GLU LYS THR LEU ILE GLU LEU ALA ASP
SEQRES 6 A 178 GLU LYS GLY CYS SER LEU ILE LEU THR THR GLY GLY THR
SEQRES 7 A 178 GLY PRO ALA PRO ARG ASP VAL THR PRO GLU ALA THR GLU
SEQRES 8 A 178 ALA VAL CYS GLU LYS MET LEU PRO GLY PHE GLY GLU LEU
SEQRES 9 A 178 MET ARG GLN VAL SER LEU LYS GLN VAL PRO THR ALA ILE
SEQRES 10 A 178 LEU SER ARG GLN THR ALA GLY ILE ARG GLY SER CYS LEU
SEQRES 11 A 178 ILE VAL ASN LEU PRO GLY LYS PRO GLN SER ILE LYS VAL
SEQRES 12 A 178 CYS LEU ASP ALA VAL MET PRO ALA ILE PRO TYR CYS ILE
SEQRES 13 A 178 ASP LEU ILE GLY GLY ALA TYR ILE ASP THR ASP PRO ASN
SEQRES 14 A 178 LYS VAL LYS ALA PHE ARG PRO LYS LYS
SEQRES 1 B 178 MET SER GLU LYS LYS ALA VAL ILE GLY VAL VAL THR ILE
SEQRES 2 B 178 SER ASP ARG ALA SER LYS GLY ILE TYR GLU ASP ILE SER
SEQRES 3 B 178 GLY LYS ALA ILE ILE ASP TYR LEU LYS ASP VAL ILE ILE
SEQRES 4 B 178 THR PRO PHE GLU VAL GLU TYR ARG VAL ILE PRO ASP GLU
SEQRES 5 B 178 ARG ASP LEU ILE GLU LYS THR LEU ILE GLU LEU ALA ASP
SEQRES 6 B 178 GLU LYS GLY CYS SER LEU ILE LEU THR THR GLY GLY THR
SEQRES 7 B 178 GLY PRO ALA PRO ARG ASP VAL THR PRO GLU ALA THR GLU
SEQRES 8 B 178 ALA VAL CYS GLU LYS MET LEU PRO GLY PHE GLY GLU LEU
SEQRES 9 B 178 MET ARG GLN VAL SER LEU LYS GLN VAL PRO THR ALA ILE
SEQRES 10 B 178 LEU SER ARG GLN THR ALA GLY ILE ARG GLY SER CYS LEU
SEQRES 11 B 178 ILE VAL ASN LEU PRO GLY LYS PRO GLN SER ILE LYS VAL
SEQRES 12 B 178 CYS LEU ASP ALA VAL MET PRO ALA ILE PRO TYR CYS ILE
SEQRES 13 B 178 ASP LEU ILE GLY GLY ALA TYR ILE ASP THR ASP PRO ASN
SEQRES 14 B 178 LYS VAL LYS ALA PHE ARG PRO LYS LYS
SEQRES 1 C 178 MET SER GLU LYS LYS ALA VAL ILE GLY VAL VAL THR ILE
SEQRES 2 C 178 SER ASP ARG ALA SER LYS GLY ILE TYR GLU ASP ILE SER
SEQRES 3 C 178 GLY LYS ALA ILE ILE ASP TYR LEU LYS ASP VAL ILE ILE
SEQRES 4 C 178 THR PRO PHE GLU VAL GLU TYR ARG VAL ILE PRO ASP GLU
SEQRES 5 C 178 ARG ASP LEU ILE GLU LYS THR LEU ILE GLU LEU ALA ASP
SEQRES 6 C 178 GLU LYS GLY CYS SER LEU ILE LEU THR THR GLY GLY THR
SEQRES 7 C 178 GLY PRO ALA PRO ARG ASP VAL THR PRO GLU ALA THR GLU
SEQRES 8 C 178 ALA VAL CYS GLU LYS MET LEU PRO GLY PHE GLY GLU LEU
SEQRES 9 C 178 MET ARG GLN VAL SER LEU LYS GLN VAL PRO THR ALA ILE
SEQRES 10 C 178 LEU SER ARG GLN THR ALA GLY ILE ARG GLY SER CYS LEU
SEQRES 11 C 178 ILE VAL ASN LEU PRO GLY LYS PRO GLN SER ILE LYS VAL
SEQRES 12 C 178 CYS LEU ASP ALA VAL MET PRO ALA ILE PRO TYR CYS ILE
SEQRES 13 C 178 ASP LEU ILE GLY GLY ALA TYR ILE ASP THR ASP PRO ASN
SEQRES 14 C 178 LYS VAL LYS ALA PHE ARG PRO LYS LYS
HET EDO A 179 4
HET EDO A 180 4
HET PEG A 181 7
HET PEG A 182 7
HET EDO C 179 4
HET EDO C 180 4
HET EDO C 181 4
HET EDO C 182 4
HETNAM EDO 1,2-ETHANEDIOL
HETNAM PEG DI(HYDROXYETHYL)ETHER
HETSYN EDO ETHYLENE GLYCOL
FORMUL 4 EDO 6(C2 H6 O2)
FORMUL 6 PEG 2(C4 H10 O3)
FORMUL 12 HOH *625(H2 O)
HELIX 1 1 SER A 14 LYS A 19 1 6
HELIX 2 2 ASP A 24 ILE A 38 1 15
HELIX 3 3 GLU A 52 GLU A 66 1 15
HELIX 4 4 VAL A 85 CYS A 94 1 10
HELIX 5 5 LEU A 98 LYS A 111 1 14
HELIX 6 6 VAL A 113 SER A 119 5 7
HELIX 7 7 LYS A 137 MET A 149 1 13
HELIX 8 8 ALA A 151 ILE A 159 1 9
HELIX 9 9 ARG B 16 GLY B 20 5 5
HELIX 10 10 ASP B 24 ILE B 38 1 15
HELIX 11 11 GLU B 52 GLU B 66 1 15
HELIX 12 12 VAL B 85 CYS B 94 1 10
HELIX 13 13 LEU B 98 LEU B 110 1 13
HELIX 14 14 LYS B 111 GLN B 112 5 2
HELIX 15 15 VAL B 113 SER B 119 5 7
HELIX 16 16 LYS B 137 MET B 149 1 13
HELIX 17 17 ALA B 151 GLY B 160 1 10
HELIX 18 18 SER C 14 GLY C 20 1 7
HELIX 19 19 ASP C 24 ILE C 38 1 15
HELIX 20 20 GLU C 52 GLU C 66 1 15
HELIX 21 21 VAL C 85 CYS C 94 1 10
HELIX 22 22 LEU C 98 LYS C 111 1 14
HELIX 23 23 GLN C 112 SER C 119 5 8
HELIX 24 24 LYS C 137 MET C 149 1 13
HELIX 25 25 ALA C 151 ILE C 159 1 9
SHEET 1 A 6 GLU A 43 ILE A 49 0
SHEET 2 A 6 VAL A 7 ILE A 13 1 N ILE A 8 O GLU A 43
SHEET 3 A 6 LEU A 71 THR A 75 1 O LEU A 71 N GLY A 9
SHEET 4 A 6 CYS A 129 LEU A 134 1 O VAL A 132 N ILE A 72
SHEET 5 A 6 ALA A 123 ARG A 126 -1 N GLY A 124 O ILE A 131
SHEET 6 A 6 LYS A 96 MET A 97 -1 N LYS A 96 O ILE A 125
SHEET 1 B 6 GLU B 43 ILE B 49 0
SHEET 2 B 6 VAL B 7 ILE B 13 1 N ILE B 8 O GLU B 43
SHEET 3 B 6 LEU B 71 THR B 75 1 O LEU B 71 N GLY B 9
SHEET 4 B 6 CYS B 129 LEU B 134 1 O VAL B 132 N ILE B 72
SHEET 5 B 6 ALA B 123 ARG B 126 -1 N GLY B 124 O ILE B 131
SHEET 6 B 6 LYS B 96 MET B 97 -1 N LYS B 96 O ILE B 125
SHEET 1 C 6 GLU C 43 ILE C 49 0
SHEET 2 C 6 VAL C 7 ILE C 13 1 N THR C 12 O ARG C 47
SHEET 3 C 6 LEU C 71 THR C 75 1 O LEU C 71 N GLY C 9
SHEET 4 C 6 CYS C 129 LEU C 134 1 O LEU C 134 N THR C 74
SHEET 5 C 6 ALA C 123 ARG C 126 -1 N GLY C 124 O ILE C 131
SHEET 6 C 6 LYS C 96 MET C 97 -1 N LYS C 96 O ILE C 125
SITE 1 AC1 5 PRO A 135 GLY A 136 LYS A 137 SER A 140
SITE 2 AC1 5 HOH A 699
SITE 1 AC2 7 ALA A 64 ASP A 65 ARG A 126 GLY A 127
SITE 2 AC2 7 SER A 128 HOH A 355 HOH A 467
SITE 1 AC3 5 GLU A 91 CYS A 94 GLU A 95 MET A 97
SITE 2 AC3 5 HOH A 363
SITE 1 AC4 13 PRO A 99 GLY A 102 GLU A 103 ARG A 106
SITE 2 AC4 13 GLN A 121 THR A 122 HOH A 209 HOH A 392
SITE 3 AC4 13 HOH A 441 HOH A 674 HOH A 740 GLU B 103
SITE 4 AC4 13 GLU C 103
SITE 1 AC5 3 ASP C 24 LYS C 28 TYR C 46
SITE 1 AC6 6 VAL C 93 CYS C 94 GLU C 95 ARG C 126
SITE 2 AC6 6 HOH C 686 HOH C 728
SITE 1 AC7 6 ALA C 81 PRO C 82 ARG C 83 HOH C 306
SITE 2 AC7 6 HOH C 423 HOH C 462
CRYST1 39.409 113.159 55.980 90.00 93.39 90.00 P 1 21 1 6
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 0.025375 0.000000 0.001505 0.00000
SCALE2 0.000000 0.008837 0.000000 0.00000
SCALE3 0.000000 0.000000 0.017895 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
