HEADER ISOMERASE 10-DEC-09 3ABF
TITLE CRYSTAL STRUCTURE OF A 4-OXALOCROTONATE TAUTOMERASE HOMOLOGUE
TITLE 2 (TTHB242)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: 4-OXALOCROTONATE TAUTOMERASE;
COMPND 3 CHAIN: A, B, C, D, E, F;
COMPND 4 EC: 5.3.2.2;
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: TTHB242;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET11A
KEYWDS TAUTOMERASE, ISOMERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR H.KIDA,K.MIKI
REVDAT 3 01-NOV-23 3ABF 1 REMARK
REVDAT 2 11-OCT-17 3ABF 1 REMARK
REVDAT 1 15-DEC-10 3ABF 0
JRNL AUTH H.KIDA,A.KITA,K.MIKI
JRNL TITL CRYSTAL STRUCTURE OF A 4-OXALOCROTONATE TAUTOMERASE
JRNL TITL 2 HOMOLOGUE (TTHB242) FROM THERMUS THERMOPHILUS HB8
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.94 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS
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) : 1.94
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 43.52
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) (%) : 99.7
REMARK 3 NUMBER OF REFLECTIONS : 26662
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : NULL
REMARK 3 R VALUE (WORKING SET) : 0.193
REMARK 3 FREE R VALUE : 0.228
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 1371
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
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) : NULL
REMARK 3 BIN RESOLUTION RANGE LOW (A) : NULL
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : NULL
REMARK 3 BIN FREE R VALUE : NULL
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : NULL
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3015
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 15
REMARK 3 SOLVENT ATOMS : 195
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 33.33
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.66400
REMARK 3 B22 (A**2) : -1.10900
REMARK 3 B33 (A**2) : 1.77400
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 COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM SIGMAA (A) : NULL
REMARK 3 LOW RESOLUTION CUTOFF (A) : NULL
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM C-V SIGMAA (A) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : NULL
REMARK 3 BOND ANGLES (DEGREES) : NULL
REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL
REMARK 3 IMPROPER ANGLES (DEGREES) : NULL
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) : 4.265 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 5.437 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 6.763 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 9.055 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : NULL
REMARK 3 KSOL : NULL
REMARK 3 BSOL : 67.79
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 : CNS_TOPPAR:PROTEIN_REP.PARAM
REMARK 3 PARAMETER FILE 2 : CNS_TOPPAR:WATER_REP.PARAM
REMARK 3 PARAMETER FILE 3 : CNS_TOPPAR:ION.PARAM
REMARK 3 PARAMETER FILE 4 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3 TOPOLOGY FILE 2 : NULL
REMARK 3 TOPOLOGY FILE 3 : NULL
REMARK 3 TOPOLOGY FILE 4 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 3ABF COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 11-DEC-09.
REMARK 100 THE DEPOSITION ID IS D_1000029046.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 12-OCT-02
REMARK 200 TEMPERATURE (KELVIN) : 293
REMARK 200 PH : 5.6
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : PHOTON FACTORY
REMARK 200 BEAMLINE : BL-6A
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.978
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 4R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO, HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK, HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 26856
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.940
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 (%) : 99.7
REMARK 200 DATA REDUNDANCY : 4.000
REMARK 200 R MERGE (I) : 0.05700
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 22.2310
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.94
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.01
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.3
REMARK 200 DATA REDUNDANCY IN SHELL : 3.80
REMARK 200 R MERGE FOR SHELL (I) : 0.29200
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: PDB ENTRY 1BJP
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 37.53
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.97
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.6M MGSO4, 0.1M SODIUM CITRATE PH
REMARK 280 5.6, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 290K
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 27.61350
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 44.95300
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 35.33800
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 44.95300
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 27.61350
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 35.33800
REMARK 290 SMTRY3 4 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: HEXAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 13810 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 15480 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -52.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F
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 THR B 64
REMARK 465 THR C 64
REMARK 465 GLY D 63
REMARK 465 THR D 64
REMARK 465 GLU E 62
REMARK 465 GLY E 63
REMARK 465 THR E 64
REMARK 465 THR F 64
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 ARG A 23 CG CD NE CZ NH1 NH2
REMARK 470 MET A 27 CG SD CE
REMARK 470 LYS B 16 CG CD CE NZ
REMARK 470 ARG B 22 CG CD NE CZ NH1 NH2
REMARK 470 MET B 27 CG SD CE
REMARK 470 ARG D 30 CG CD NE CZ NH1 NH2
REMARK 470 LYS D 61 CG CD CE NZ
REMARK 470 GLU D 62 CG CD OE1 OE2
REMARK 470 GLU E 26 CG CD OE1 OE2
REMARK 470 ARG E 30 CG CD NE CZ NH1 NH2
REMARK 470 GLU E 37 CG CD OE1 OE2
REMARK 470 LYS E 61 CG CD CE NZ
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 ARG F 30 -72.50 -60.72
REMARK 500 LYS F 61 111.68 -23.10
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 SO4 A 71
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C 70
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 E 72
DBREF 3ABF A 1 64 UNP Q53WI4 Q53WI4_THET8 1 64
DBREF 3ABF B 1 64 UNP Q53WI4 Q53WI4_THET8 1 64
DBREF 3ABF C 1 64 UNP Q53WI4 Q53WI4_THET8 1 64
DBREF 3ABF D 1 64 UNP Q53WI4 Q53WI4_THET8 1 64
DBREF 3ABF E 1 64 UNP Q53WI4 Q53WI4_THET8 1 64
DBREF 3ABF F 1 64 UNP Q53WI4 Q53WI4_THET8 1 64
SEQRES 1 A 64 MET VAL VAL LEU LYS VAL THR LEU LEU GLU GLY ARG PRO
SEQRES 2 A 64 PRO GLU LYS LYS ARG GLU LEU VAL ARG ARG LEU THR GLU
SEQRES 3 A 64 MET ALA SER ARG LEU LEU GLY GLU PRO TYR GLU GLU VAL
SEQRES 4 A 64 ARG VAL ILE LEU TYR GLU VAL ARG ARG ASP GLN TRP ALA
SEQRES 5 A 64 ALA GLY GLY VAL LEU PHE SER ASP LYS GLU GLY THR
SEQRES 1 B 64 MET VAL VAL LEU LYS VAL THR LEU LEU GLU GLY ARG PRO
SEQRES 2 B 64 PRO GLU LYS LYS ARG GLU LEU VAL ARG ARG LEU THR GLU
SEQRES 3 B 64 MET ALA SER ARG LEU LEU GLY GLU PRO TYR GLU GLU VAL
SEQRES 4 B 64 ARG VAL ILE LEU TYR GLU VAL ARG ARG ASP GLN TRP ALA
SEQRES 5 B 64 ALA GLY GLY VAL LEU PHE SER ASP LYS GLU GLY THR
SEQRES 1 C 64 MET VAL VAL LEU LYS VAL THR LEU LEU GLU GLY ARG PRO
SEQRES 2 C 64 PRO GLU LYS LYS ARG GLU LEU VAL ARG ARG LEU THR GLU
SEQRES 3 C 64 MET ALA SER ARG LEU LEU GLY GLU PRO TYR GLU GLU VAL
SEQRES 4 C 64 ARG VAL ILE LEU TYR GLU VAL ARG ARG ASP GLN TRP ALA
SEQRES 5 C 64 ALA GLY GLY VAL LEU PHE SER ASP LYS GLU GLY THR
SEQRES 1 D 64 MET VAL VAL LEU LYS VAL THR LEU LEU GLU GLY ARG PRO
SEQRES 2 D 64 PRO GLU LYS LYS ARG GLU LEU VAL ARG ARG LEU THR GLU
SEQRES 3 D 64 MET ALA SER ARG LEU LEU GLY GLU PRO TYR GLU GLU VAL
SEQRES 4 D 64 ARG VAL ILE LEU TYR GLU VAL ARG ARG ASP GLN TRP ALA
SEQRES 5 D 64 ALA GLY GLY VAL LEU PHE SER ASP LYS GLU GLY THR
SEQRES 1 E 64 MET VAL VAL LEU LYS VAL THR LEU LEU GLU GLY ARG PRO
SEQRES 2 E 64 PRO GLU LYS LYS ARG GLU LEU VAL ARG ARG LEU THR GLU
SEQRES 3 E 64 MET ALA SER ARG LEU LEU GLY GLU PRO TYR GLU GLU VAL
SEQRES 4 E 64 ARG VAL ILE LEU TYR GLU VAL ARG ARG ASP GLN TRP ALA
SEQRES 5 E 64 ALA GLY GLY VAL LEU PHE SER ASP LYS GLU GLY THR
SEQRES 1 F 64 MET VAL VAL LEU LYS VAL THR LEU LEU GLU GLY ARG PRO
SEQRES 2 F 64 PRO GLU LYS LYS ARG GLU LEU VAL ARG ARG LEU THR GLU
SEQRES 3 F 64 MET ALA SER ARG LEU LEU GLY GLU PRO TYR GLU GLU VAL
SEQRES 4 F 64 ARG VAL ILE LEU TYR GLU VAL ARG ARG ASP GLN TRP ALA
SEQRES 5 F 64 ALA GLY GLY VAL LEU PHE SER ASP LYS GLU GLY THR
HET SO4 A 71 5
HET SO4 C 70 5
HET SO4 E 72 5
HETNAM SO4 SULFATE ION
FORMUL 7 SO4 3(O4 S 2-)
FORMUL 10 HOH *195(H2 O)
HELIX 1 1 PRO A 13 LEU A 32 1 20
HELIX 2 2 PRO A 35 GLU A 37 5 3
HELIX 3 3 ARG A 47 ASP A 49 5 3
HELIX 4 4 PHE A 58 GLU A 62 1 5
HELIX 5 5 PRO B 13 LEU B 32 1 20
HELIX 6 6 PRO B 35 GLU B 37 5 3
HELIX 7 7 ARG B 47 ASP B 49 5 3
HELIX 8 8 SER B 59 LYS B 61 5 3
HELIX 9 9 PRO C 13 GLY C 33 1 21
HELIX 10 10 PRO C 35 GLU C 37 5 3
HELIX 11 11 ARG C 47 ASP C 49 5 3
HELIX 12 12 PHE C 58 GLY C 63 1 6
HELIX 13 13 PRO D 13 GLY D 33 1 21
HELIX 14 14 PRO D 35 GLU D 37 5 3
HELIX 15 15 ARG D 47 ASP D 49 5 3
HELIX 16 16 PHE D 58 GLU D 62 1 5
HELIX 17 17 PRO E 13 GLY E 33 1 21
HELIX 18 18 PRO E 35 GLU E 37 5 3
HELIX 19 19 ARG E 47 ASP E 49 5 3
HELIX 20 20 SER E 59 LYS E 61 5 3
HELIX 21 21 PRO F 13 GLY F 33 1 21
HELIX 22 22 PRO F 35 GLU F 37 5 3
HELIX 23 23 ARG F 47 ASP F 49 5 3
HELIX 24 24 SER F 59 LYS F 61 5 3
SHEET 1 A 8 VAL D 56 LEU D 57 0
SHEET 2 A 8 TRP D 51 ALA D 53 -1 N ALA D 53 O VAL D 56
SHEET 3 A 8 VAL B 39 VAL B 46 -1 N VAL B 41 O ALA D 52
SHEET 4 A 8 VAL B 2 LEU B 9 1 N VAL B 6 O TYR B 44
SHEET 5 A 8 VAL A 2 LEU A 9 -1 N THR A 7 O VAL B 3
SHEET 6 A 8 VAL A 39 VAL A 46 1 O ILE A 42 N VAL A 6
SHEET 7 A 8 TRP E 51 ALA E 53 -1 O ALA E 52 N VAL A 41
SHEET 8 A 8 VAL E 56 LEU E 57 -1 O VAL E 56 N ALA E 53
SHEET 1 B 8 VAL A 56 LEU A 57 0
SHEET 2 B 8 TRP A 51 ALA A 53 -1 N ALA A 53 O VAL A 56
SHEET 3 B 8 VAL C 39 VAL C 46 -1 O VAL C 41 N ALA A 52
SHEET 4 B 8 VAL C 2 LEU C 9 1 N VAL C 6 O TYR C 44
SHEET 5 B 8 VAL D 2 LEU D 9 -1 O THR D 7 N VAL C 3
SHEET 6 B 8 VAL D 39 VAL D 46 1 O TYR D 44 N VAL D 6
SHEET 7 B 8 TRP F 51 ALA F 53 -1 O ALA F 52 N VAL D 41
SHEET 8 B 8 VAL F 56 LEU F 57 -1 O VAL F 56 N ALA F 53
SHEET 1 C 8 VAL B 56 LEU B 57 0
SHEET 2 C 8 TRP B 51 ALA B 53 -1 N ALA B 53 O VAL B 56
SHEET 3 C 8 VAL F 39 VAL F 46 -1 O VAL F 41 N ALA B 52
SHEET 4 C 8 VAL F 2 LEU F 9 1 N VAL F 6 O TYR F 44
SHEET 5 C 8 VAL E 2 LEU E 9 -1 N VAL E 3 O THR F 7
SHEET 6 C 8 VAL E 39 VAL E 46 1 O ARG E 40 N LEU E 4
SHEET 7 C 8 TRP C 51 ALA C 53 -1 N ALA C 52 O VAL E 41
SHEET 8 C 8 VAL C 56 LEU C 57 -1 O VAL C 56 N ALA C 53
SITE 1 AC1 10 LYS A 5 HOH A 159 HOH A 195 HOH A 224
SITE 2 AC1 10 HOH A 282 LYS B 5 LYS C 5 SO4 C 70
SITE 3 AC1 10 LYS D 5 HOH D 228
SITE 1 AC2 10 SO4 A 71 LYS C 5 HOH C 139 HOH C 143
SITE 2 AC2 10 HOH C 250 HOH C 279 LYS D 5 LYS E 5
SITE 3 AC2 10 SO4 E 72 LYS F 5
SITE 1 AC3 9 LYS A 5 LYS B 5 SO4 C 70 LYS E 5
SITE 2 AC3 9 HOH E 138 HOH E 155 HOH E 226 HOH E 231
SITE 3 AC3 9 LYS F 5
CRYST1 55.227 70.676 89.906 90.00 90.00 90.00 P 21 21 21 24
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 0.018107 0.000000 0.000000 0.00000
SCALE2 0.000000 0.014149 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011123 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
