HEADER TRANSFERASE 30-DEC-09 3ACB
TITLE CRYSTAL STRUCTURE OF HYPOXANTHINE-GUANINE PHOSPHORIBOSYLTRANSFERASE
TITLE 2 FROM THERMUS THERMOPHILUS HB8
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HYPOXANTHINE-GUANINE PHOSPHORIBOSYLTRANSFERASE;
COMPND 3 CHAIN: A;
COMPND 4 EC: 2.4.2.8;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: THERMUS THERMOPHILUS;
SOURCE 3 ORGANISM_TAXID: 300852;
SOURCE 4 STRAIN: HB8;
SOURCE 5 GENE: TTHA0220;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET-11A
KEYWDS ROSSMANN FOLD, STRUCTURAL GENOMICS, NPPSFA, NATIONAL PROJECT ON
KEYWDS 2 PROTEIN STRUCTURAL AND FUNCTIONAL ANALYSES, RIKEN STRUCTURAL
KEYWDS 3 GENOMICS/PROTEOMICS INITIATIVE, RSGI, GLYCOSYLTRANSFERASE,
KEYWDS 4 TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR M.KANAGAWA,S.BABA,K.HIROTSU,S.KURAMITSU,S.YOKOYAMA,G.KAWAI,G.SAMPEI,
AUTHOR 2 RIKEN STRUCTURAL GENOMICS/PROTEOMICS INITIATIVE (RSGI)
REVDAT 4 01-NOV-23 3ACB 1 REMARK
REVDAT 3 08-SEP-10 3ACB 1 JRNL
REVDAT 2 23-FEB-10 3ACB 1 SPRSDE
REVDAT 1 09-FEB-10 3ACB 0
SPRSDE 23-FEB-10 3ACB 2YWS
JRNL AUTH M.KANAGAWA,S.BABA,A.EBIHARA,A.SHINKAI,K.HIROTSU,R.MEGA,
JRNL AUTH 2 K.KIM,S.KURAMITSU,G.SAMPEI,G.KAWAI
JRNL TITL STRUCTURES OF HYPOXANTHINE-GUANINE PHOSPHORIBOSYLTRANSFERASE
JRNL TITL 2 (TTHA0220) FROM THERMUS THERMOPHILUS HB8.
JRNL REF ACTA CRYSTALLOGR.,SECT.F V. 66 893 2010
JRNL REFN ESSN 1744-3091
JRNL PMID 20693661
JRNL DOI 10.1107/S1744309110023079
REMARK 2
REMARK 2 RESOLUTION. 2.06 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.1
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 : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.06
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 46.06
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 105374.820
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 98.4
REMARK 3 NUMBER OF REFLECTIONS : 12932
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) : 0.201
REMARK 3 FREE R VALUE : 0.228
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 10.300
REMARK 3 FREE R VALUE TEST SET COUNT : 1326
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.006
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) : 2.06
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.19
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 95.80
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 1822
REMARK 3 BIN R VALUE (WORKING SET) : 0.2080
REMARK 3 BIN FREE R VALUE : 0.2630
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 10.30
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 210
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.018
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1308
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 12
REMARK 3 SOLVENT ATOMS : 127
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 15.30
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 28.60
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 2.09000
REMARK 3 B22 (A**2) : 2.09000
REMARK 3 B33 (A**2) : -4.19000
REMARK 3 B12 (A**2) : 1.29000
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) : 0.22
REMARK 3 ESD FROM SIGMAA (A) : 0.12
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) : 0.26
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.17
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.005
REMARK 3 BOND ANGLES (DEGREES) : 1.300
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 22.90
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.820
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 : 0.36
REMARK 3 BSOL : 53.17
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 : DIO.PARAM
REMARK 3 PARAMETER FILE 4 : CIS_PEPTIDE.PARAM
REMARK 3 PARAMETER FILE 5 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : WATER_REP.TOP
REMARK 3 TOPOLOGY FILE 3 : DIO.TOP
REMARK 3 TOPOLOGY FILE 4 : NULL
REMARK 3 TOPOLOGY FILE 5 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 3ACB COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 07-JAN-10.
REMARK 100 THE DEPOSITION ID IS D_1000029077.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 18-MAR-07
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SPRING-8
REMARK 200 BEAMLINE : BL26B1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0000
REMARK 200 MONOCHROMATOR : FIXED EXIT SI DOUBLE CRYSTAL
REMARK 200 MONOCHROMATOR
REMARK 200 OPTICS : NULL
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 : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 12932
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.060
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 200 DATA REDUNDANCY : 10.80
REMARK 200 R MERGE (I) : 0.08800
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) : 2.06
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.13
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.3
REMARK 200 DATA REDUNDANCY IN SHELL : 7.90
REMARK 200 R MERGE FOR SHELL (I) : 0.31900
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: 1YFZ
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 49.31
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.43
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 15% GLYCEROL, 38% DIOXANE, PH 8.0,
REMARK 280 VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 65 2 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+2/3
REMARK 290 3555 -X+Y,-X,Z+1/3
REMARK 290 4555 -X,-Y,Z+1/2
REMARK 290 5555 Y,-X+Y,Z+1/6
REMARK 290 6555 X-Y,X,Z+5/6
REMARK 290 7555 Y,X,-Z+2/3
REMARK 290 8555 X-Y,-Y,-Z
REMARK 290 9555 -X,-X+Y,-Z+1/3
REMARK 290 10555 -Y,-X,-Z+1/6
REMARK 290 11555 -X+Y,Y,-Z+1/2
REMARK 290 12555 X,X-Y,-Z+5/6
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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 101.70467
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 50.85233
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 76.27850
REMARK 290 SMTRY1 5 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 5 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 25.42617
REMARK 290 SMTRY1 6 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 127.13083
REMARK 290 SMTRY1 7 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 7 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 101.70467
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 9 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 9 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 9 0.000000 0.000000 -1.000000 50.85233
REMARK 290 SMTRY1 10 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 10 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 10 0.000000 0.000000 -1.000000 25.42617
REMARK 290 SMTRY1 11 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 11 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 11 0.000000 0.000000 -1.000000 76.27850
REMARK 290 SMTRY1 12 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 12 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 12 0.000000 0.000000 -1.000000 127.13083
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2910 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 14320 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -19.0 KCAL/MOL
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 BIOMT1 2 0.500000 -0.866025 0.000000 33.35600
REMARK 350 BIOMT2 2 -0.866025 -0.500000 0.000000 57.77429
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 25.42617
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 LYS A 2
REMARK 465 SER A 72
REMARK 465 TYR A 73
REMARK 465 GLY A 74
REMARK 465 ASN A 75
REMARK 465 ALA A 76
REMARK 465 PHE A 77
REMARK 465 LYS A 78
REMARK 465 SER A 79
REMARK 465 SER A 80
REMARK 465 GLY A 81
REMARK 465 GLU A 82
REMARK 465 VAL A 83
REMARK 465 GLU A 181
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 MET A 4 0.18 -163.46
REMARK 500 ASP A 106 -75.58 -113.25
REMARK 500 LYS A 134 79.29 -115.20
REMARK 500 GLN A 165 -15.12 79.18
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DIO A 791
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DIO A 792
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3ACC RELATED DB: PDB
REMARK 900 RELATED ID: 3ACD RELATED DB: PDB
DBREF 3ACB A 1 181 UNP Q5SLS3 Q5SLS3_THET8 1 181
SEQRES 1 A 181 MET LYS GLY MET PHE THR PRO GLY ASN GLY PRO VAL GLN
SEQRES 2 A 181 ILE SER ALA GLU ALA ILE LYS LYS ARG VAL GLU GLU LEU
SEQRES 3 A 181 GLY GLY GLU ILE ALA ARG ASP TYR GLN GLY LYS THR PRO
SEQRES 4 A 181 HIS LEU ILE CYS VAL LEU ASN GLY ALA PHE ILE PHE MET
SEQRES 5 A 181 ALA ASP LEU VAL ARG ALA ILE PRO LEU PRO LEU THR MET
SEQRES 6 A 181 ASP PHE ILE ALA ILE SER SER TYR GLY ASN ALA PHE LYS
SEQRES 7 A 181 SER SER GLY GLU VAL GLU LEU LEU LYS ASP LEU ARG LEU
SEQRES 8 A 181 PRO ILE HIS GLY ARG ASP VAL ILE VAL VAL GLU ASP ILE
SEQRES 9 A 181 VAL ASP THR GLY LEU THR LEU SER TYR LEU LEU ASP TYR
SEQRES 10 A 181 LEU GLU ALA ARG LYS PRO ALA SER VAL ARG VAL ALA ALA
SEQRES 11 A 181 LEU LEU SER LYS PRO SER ARG ARG GLN VAL GLU VAL PRO
SEQRES 12 A 181 ILE HIS TYR LEU GLY PHE GLU ILE GLU ASP ALA TYR VAL
SEQRES 13 A 181 TYR GLY TYR GLY LEU ASP ARG ALA GLN PHE ASP ARG ASN
SEQRES 14 A 181 LEU PRO PHE ILE THR SER ILE ARG PRO GLU GLU GLU
HET DIO A 791 6
HET DIO A 792 6
HETNAM DIO 1,4-DIETHYLENE DIOXIDE
FORMUL 2 DIO 2(C4 H8 O2)
FORMUL 4 HOH *127(H2 O)
HELIX 1 1 SER A 15 TYR A 34 1 20
HELIX 2 2 ALA A 48 ARG A 57 1 10
HELIX 3 3 GLY A 108 ALA A 120 1 13
HELIX 4 4 PRO A 135 ARG A 138 5 4
SHEET 1 A 5 THR A 64 ALA A 69 0
SHEET 2 A 5 PRO A 39 LEU A 45 1 N LEU A 45 O ILE A 68
SHEET 3 A 5 ASP A 97 VAL A 105 1 O VAL A 101 N ILE A 42
SHEET 4 A 5 SER A 125 SER A 133 1 O ALA A 129 N VAL A 100
SHEET 5 A 5 TYR A 146 GLU A 150 1 O GLY A 148 N ALA A 130
SHEET 1 B 2 TYR A 155 TYR A 157 0
SHEET 2 B 2 THR A 174 ILE A 176 -1 O THR A 174 N TYR A 157
CISPEP 1 LEU A 45 ASN A 46 0 -0.30
SITE 1 AC1 6 ASP A 33 TYR A 34 LYS A 37 SER A 125
SITE 2 AC1 6 ARG A 127 HOH A 917
SITE 1 AC2 6 MET A 4 PHE A 5 PRO A 60 LEU A 61
SITE 2 AC2 6 PRO A 62 ASP A 167
CRYST1 66.712 66.712 152.557 90.00 90.00 120.00 P 65 2 2 12
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 0.014990 0.008654 0.000000 0.00000
SCALE2 0.000000 0.017309 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006555 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
