HEADER ISOMERASE 06-MAR-10 3M20
TITLE CRYSTAL STRUCTURE OF DMPI FROM ARCHAEOGLOBUS FULGIDUS DETERMINED TO
TITLE 2 2.37 ANGSTROMS RESOLUTION
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: 4-OXALOCROTONATE TAUTOMERASE, PUTATIVE;
COMPND 3 CHAIN: A, B, C;
COMPND 4 EC: 5.3.2.2;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ARCHAEOGLOBUS FULGIDUS;
SOURCE 3 ORGANISM_TAXID: 224325;
SOURCE 4 STRAIN: DSM 4304;
SOURCE 5 GENE: AF_0669, DMPI;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: JM109;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET24A(+)
KEYWDS 4-OXALOCROTONATE TAUTOMERASE, ARCHAEOGLOBUS FULGIDUS, DMPI,
KEYWDS 2 THERMOPHILE, BETA-ALPHA-BETA, CATALYTIC PROLINE, ISOMERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR M.L.HACKERT,C.P.WHITMAN,J.J.ALMRUD,R.DASGUPTA,A.D.KERN
REVDAT 4 06-SEP-23 3M20 1 REMARK
REVDAT 3 08-NOV-17 3M20 1 REMARK
REVDAT 2 10-NOV-10 3M20 1 JRNL
REVDAT 1 01-SEP-10 3M20 0
JRNL AUTH J.J.ALMRUD,R.DASGUPTA,R.M.CZERWINSKI,A.D.KERN,M.L.HACKERT,
JRNL AUTH 2 C.P.WHITMAN
JRNL TITL KINETIC AND STRUCTURAL CHARACTERIZATION OF DMPI FROM
JRNL TITL 2 HELICOBACTER PYLORI AND ARCHAEOGLOBUS FULGIDUS, TWO
JRNL TITL 3 4-OXALOCROTONATE TAUTOMERASE FAMILY MEMBERS.
JRNL REF BIOORG.CHEM. V. 38 252 2010
JRNL REFN ISSN 0045-2068
JRNL PMID 20709352
JRNL DOI 10.1016/J.BIOORG.2010.07.002
REMARK 2
REMARK 2 RESOLUTION. 2.37 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 : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.37
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 24.53
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 93.0
REMARK 3 NUMBER OF REFLECTIONS : 6674
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) : 0.296
REMARK 3 FREE R VALUE : 0.316
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.700
REMARK 3 FREE R VALUE TEST SET COUNT : 317
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.018
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : NULL
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.37
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.48
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 90.80
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 760
REMARK 3 BIN R VALUE (WORKING SET) : 0.4040
REMARK 3 BIN FREE R VALUE : 0.4430
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 4.40
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 35
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.075
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1267
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 20
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 33.60
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 46.78
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -11.41000
REMARK 3 B22 (A**2) : -11.41000
REMARK 3 B33 (A**2) : 22.82000
REMARK 3 B12 (A**2) : -6.48000
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) : 0.44
REMARK 3 ESD FROM SIGMAA (A) : 0.51
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) : 0.52
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.70
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.008
REMARK 3 BOND ANGLES (DEGREES) : 1.300
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 27.40
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.760
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : NULL
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 : CNS BULK SOLVENT MODEL USED
REMARK 3 KSOL : 0.33
REMARK 3 BSOL : 56.04
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 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 3M20 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 09-MAR-10.
REMARK 100 THE DEPOSITION ID IS D_1000058007.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 10-OCT-00
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
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 RU200
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS IV
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO, HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 8623
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.290
REMARK 200 RESOLUTION RANGE LOW (A) : 24.530
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.4
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : 0.06400
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 14.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.29
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.37
REMARK 200 COMPLETENESS FOR SHELL (%) : 97.4
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.47500
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: AMORE
REMARK 200 STARTING MODEL: PDB ENTRY 1BJP
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 37.78
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.98
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 28 % PEG400, 200MM CACL2, 0.1M HEPES
REMARK 280 (PH 7.5), VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32 2 1
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 Y,X,-Z
REMARK 290 5555 X-Y,-Y,-Z+1/3
REMARK 290 6555 -X,-X+Y,-Z+2/3
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 79.16467
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 39.58233
REMARK 290 SMTRY1 4 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 4 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 5 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 39.58233
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 79.16467
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: HEXAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 13060 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 13450 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -84.0 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 350 BIOMT1 2 -0.500000 0.866025 0.000000 0.00000
REMARK 350 BIOMT2 2 0.866025 0.500000 0.000000 0.00000
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 GLU A 60
REMARK 465 ARG A 61
REMARK 465 GLU A 62
REMARK 465 ARG B 59
REMARK 465 GLU B 60
REMARK 465 ARG B 61
REMARK 465 GLU B 62
REMARK 465 ARG C 59
REMARK 465 GLU C 60
REMARK 465 ARG C 61
REMARK 465 GLU C 62
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 GLU A 20 CG CD OE1 OE2
REMARK 470 ILE A 29 CG1 CG2 CD1
REMARK 470 LYS A 54 CG CD CE NZ
REMARK 470 ARG A 59 CG CD NE CZ NH1 NH2
REMARK 470 ASP B 11 CG OD1 OD2
REMARK 470 VAL B 12 CG1 CG2
REMARK 470 GLU B 17 CG CD OE1 OE2
REMARK 470 GLU B 20 CG CD OE1 OE2
REMARK 470 THR B 23 OG1 CG2
REMARK 470 GLU B 28 CG CD OE1 OE2
REMARK 470 ILE B 29 CG1 CG2 CD1
REMARK 470 SER B 35 OG
REMARK 470 LYS B 54 CG CD CE NZ
REMARK 470 GLU C 20 CG CD OE1 OE2
REMARK 470 ILE C 29 CG1 CG2 CD1
REMARK 470 LYS C 54 CG CD CE NZ
REMARK 470 LEU C 55 CG CD1 CD2
REMARK 470 ILE C 56 CG1 CG2 CD1
REMARK 480
REMARK 480 ZERO OCCUPANCY ATOM
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 480 M RES C SSEQI ATOMS
REMARK 480 ILE A 37 CD1
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 9 108.62 -55.99
REMARK 500 ARG A 34 43.67 -84.19
REMARK 500 SER A 35 0.68 -154.28
REMARK 500 PRO B 8 166.20 -44.21
REMARK 500 LYS B 14 -18.97 -46.03
REMARK 500 SER B 24 -71.12 -59.93
REMARK 500 GLU B 28 7.02 -68.42
REMARK 500 ILE B 29 -75.58 -114.72
REMARK 500 MET B 32 -174.94 -51.22
REMARK 500 ARG B 34 -0.63 -53.63
REMARK 500 SER B 35 -89.85 -78.64
REMARK 500 ALA B 36 24.79 -59.64
REMARK 500 ALA B 46 -5.97 -52.62
REMARK 500 LEU C 55 174.12 -49.11
REMARK 500 ALA C 57 15.70 -58.80
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3M21 RELATED DB: PDB
DBREF 3M20 A 1 62 UNP O29588 O29588_ARCFU 2 63
DBREF 3M20 B 1 62 UNP O29588 O29588_ARCFU 2 63
DBREF 3M20 C 1 62 UNP O29588 O29588_ARCFU 2 63
SEQRES 1 A 62 PRO VAL LEU ILE VAL TYR GLY PRO LYS LEU ASP VAL GLY
SEQRES 2 A 62 LYS LYS ARG GLU PHE VAL GLU ARG LEU THR SER VAL ALA
SEQRES 3 A 62 ALA GLU ILE TYR GLY MET ASP ARG SER ALA ILE THR ILE
SEQRES 4 A 62 LEU ILE HIS GLU PRO PRO ALA GLU ASN VAL GLY VAL GLY
SEQRES 5 A 62 GLY LYS LEU ILE ALA ASP ARG GLU ARG GLU
SEQRES 1 B 62 PRO VAL LEU ILE VAL TYR GLY PRO LYS LEU ASP VAL GLY
SEQRES 2 B 62 LYS LYS ARG GLU PHE VAL GLU ARG LEU THR SER VAL ALA
SEQRES 3 B 62 ALA GLU ILE TYR GLY MET ASP ARG SER ALA ILE THR ILE
SEQRES 4 B 62 LEU ILE HIS GLU PRO PRO ALA GLU ASN VAL GLY VAL GLY
SEQRES 5 B 62 GLY LYS LEU ILE ALA ASP ARG GLU ARG GLU
SEQRES 1 C 62 PRO VAL LEU ILE VAL TYR GLY PRO LYS LEU ASP VAL GLY
SEQRES 2 C 62 LYS LYS ARG GLU PHE VAL GLU ARG LEU THR SER VAL ALA
SEQRES 3 C 62 ALA GLU ILE TYR GLY MET ASP ARG SER ALA ILE THR ILE
SEQRES 4 C 62 LEU ILE HIS GLU PRO PRO ALA GLU ASN VAL GLY VAL GLY
SEQRES 5 C 62 GLY LYS LEU ILE ALA ASP ARG GLU ARG GLU
FORMUL 4 HOH *20(H2 O)
HELIX 1 1 ASP A 11 GLY A 31 1 21
HELIX 2 2 PRO A 45 GLU A 47 5 3
HELIX 3 3 ASP B 11 GLY B 31 1 21
HELIX 4 4 ASP C 11 TYR C 30 1 20
HELIX 5 5 ASP C 33 ALA C 36 5 4
SHEET 1 A 4 VAL A 2 TYR A 6 0
SHEET 2 A 4 THR A 38 HIS A 42 1 O HIS A 42 N VAL A 5
SHEET 3 A 4 VAL B 49 VAL B 51 -1 O GLY B 50 N ILE A 39
SHEET 4 A 4 LYS B 54 LEU B 55 -1 O LYS B 54 N VAL B 51
SHEET 1 B 4 LYS A 54 LEU A 55 0
SHEET 2 B 4 VAL A 49 VAL A 51 -1 N VAL A 51 O LYS A 54
SHEET 3 B 4 THR C 38 HIS C 42 -1 O ILE C 39 N GLY A 50
SHEET 4 B 4 VAL C 2 TYR C 6 1 N VAL C 5 O HIS C 42
SHEET 1 C 4 VAL B 2 TYR B 6 0
SHEET 2 C 4 THR B 38 HIS B 42 1 O LEU B 40 N VAL B 5
SHEET 3 C 4 VAL C 49 VAL C 51 -1 O GLY C 50 N ILE B 39
SHEET 4 C 4 LYS C 54 LEU C 55 -1 O LYS C 54 N VAL C 51
CRYST1 49.070 49.070 118.747 90.00 90.00 120.00 P 32 2 1 18
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 0.020379 0.011766 0.000000 0.00000
SCALE2 0.000000 0.023532 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008421 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
