HEADER TRANSCRIPTION 16-DEC-08 3FK6
TITLE CRYSTAL STRUCTURE OF TETR TRIPLE MUTANT (H64K, S135L, S138I)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TETRACYCLINE REPRESSOR PROTEIN CLASS B FROM TRANSPOSON
COMPND 3 TN10, TETRACYCLINE REPRESSOR PROTEIN CLASS D;
COMPND 4 CHAIN: A, B;
COMPND 5 FRAGMENT: DNA-BINDING DOMAIN (RESIDUES 1-50) AND THE EFFECTOR-BINDING
COMPND 6 DOMAIN (RESIDUES 51-208);
COMPND 7 ENGINEERED: YES;
COMPND 8 MUTATION: YES;
COMPND 9 OTHER_DETAILS: THE FUSION PROTEIN OF DNA-BINDING DOMAIN (RESIDUES 1-
COMPND 10 50) FROM TETR VARIANT B AND THE EFFECTOR-BINDING DOMAIN (RESIDUES 51-
COMPND 11 208) FROM TETR VARIANT D
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 562;
SOURCE 4 STRAIN: K12;
SOURCE 5 GENE: TETR;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: RB791;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PWH610
KEYWDS TETRACYCLINE REPRESSOR, BACTERIAL TRANSCRIPTION REGULATION, ALTERED
KEYWDS 2 INDUCER SPECIFICITY, 4-DE-DIMETHYLAMINO-ANHYDROTETRACYCLINE,
KEYWDS 3 ANTIBIOTIC RESISTANCE, DNA-BINDING, MAGNESIUM, METAL-BINDING,
KEYWDS 4 REPRESSOR, TRANSCRIPTION, TRANSCRIPTION REGULATION, TRANSPOSABLE
KEYWDS 5 ELEMENT
EXPDTA X-RAY DIFFRACTION
AUTHOR M.A.KLIEBER,O.SCHOLZ,S.LOCHNER,P.GMEINER,W.HILLEN,Y.A.MULLER
REVDAT 5 01-NOV-23 3FK6 1 REMARK
REVDAT 4 10-NOV-21 3FK6 1 SEQADV
REVDAT 3 01-NOV-17 3FK6 1 REMARK
REVDAT 2 23-AUG-17 3FK6 1 SOURCE
REVDAT 1 27-OCT-09 3FK6 0
JRNL AUTH M.A.KLIEBER,O.SCHOLZ,S.LOCHNER,P.GMEINER,W.HILLEN,Y.A.MULLER
JRNL TITL STRUCTURAL ORIGINS FOR SELECTIVITY AND SPECIFICITY IN AN
JRNL TITL 2 ENGINEERED BACTERIAL REPRESSOR-INDUCER PAIR.
JRNL REF FEBS J. V. 276 5610 2009
JRNL REFN ISSN 1742-464X
JRNL PMID 19712110
JRNL DOI 10.1111/J.1742-4658.2009.07254.X
REMARK 2
REMARK 2 RESOLUTION. 2.10 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 : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.10
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 15.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 93.4
REMARK 3 NUMBER OF REFLECTIONS : 24749
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING SET) : 0.216
REMARK 3 FREE R VALUE : 0.262
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 7.500
REMARK 3 FREE R VALUE TEST SET COUNT : 1995
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 : 3093
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 116
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 15.10
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 43.26
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 2.57500
REMARK 3 B22 (A**2) : -5.83100
REMARK 3 B33 (A**2) : 3.25600
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.58400
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) : 0.005
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) : 1.505 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 2.388 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 2.275 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 3.464 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : NULL
REMARK 3 KSOL : NULL
REMARK 3 BSOL : 51.84
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 : DNA-RNA_REP.PARAM
REMARK 3 PARAMETER FILE 3 : WATER_REP.PARAM
REMARK 3 PARAMETER FILE 4 : ION.PARAM
REMARK 3 PARAMETER FILE 5 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : DNA-RNA.TOP
REMARK 3 TOPOLOGY FILE 3 : WATER.TOP
REMARK 3 TOPOLOGY FILE 4 : ION.TOP
REMARK 3 TOPOLOGY FILE 5 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 3FK6 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 18-DEC-08.
REMARK 100 THE DEPOSITION ID IS D_1000050689.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 18-JUN-04
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 8.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : BESSY
REMARK 200 BEAMLINE : 14.1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9797
REMARK 200 MONOCHROMATOR : SI 111 CHANNEL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MAR CCD 165 MM
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 24749
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.100
REMARK 200 RESOLUTION RANGE LOW (A) : 15.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 93.3
REMARK 200 DATA REDUNDANCY : 3.300
REMARK 200 R MERGE (I) : 0.06400
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) : 2.10
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.25
REMARK 200 COMPLETENESS FOR SHELL (%) : 95.9
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.37100
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 2TCT
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 49.44
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.43
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1M DIPOTASSIUM HYDROGEN PHOSPHATE,
REMARK 280 200MM SODIUM CHLORIDE, 50MM TRIS-HCL, PH 8.0, VAPOR DIFFUSION,
REMARK 280 HANGING DROP, TEMPERATURE 292K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y,-Z
REMARK 290 3555 X+1/2,Y+1/2,Z
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 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 63.17500
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 29.03000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 63.17500
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 29.03000
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 5470 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 18140 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -39.0 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 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 SER A 2
REMARK 465 ARG A 3
REMARK 465 THR A 156
REMARK 465 ASP A 157
REMARK 465 ARG A 158
REMARK 465 PRO A 159
REMARK 465 ALA A 160
REMARK 465 ALA A 161
REMARK 465 PRO A 162
REMARK 465 ASP A 163
REMARK 465 GLU A 164
REMARK 465 VAL A 208
REMARK 465 MET B 1
REMARK 465 SER B 2
REMARK 465 THR B 156
REMARK 465 ASP B 157
REMARK 465 ARG B 158
REMARK 465 PRO B 159
REMARK 465 ALA B 160
REMARK 465 ALA B 161
REMARK 465 PRO B 162
REMARK 465 ASP B 163
REMARK 465 LEU B 205
REMARK 465 GLN B 206
REMARK 465 ILE B 207
REMARK 465 VAL B 208
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 8 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 LYS A 6 -70.21 -39.58
REMARK 500 SER A 67 -47.39 -148.06
REMARK 500 GLU A 150 -78.29 -88.55
REMARK 500 HIS A 151 -27.22 -34.48
REMARK 500 ALA A 154 38.55 -72.93
REMARK 500 SER B 67 -43.76 -145.40
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2VKE RELATED DB: PDB
REMARK 900 RELATED ID: 2O7O RELATED DB: PDB
REMARK 900 RELATED ID: 2VKV RELATED DB: PDB
REMARK 900 RELATED ID: 2TCT RELATED DB: PDB
REMARK 900 RELATED ID: 3FK7 RELATED DB: PDB
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 THE FUSION PROTEIN OF DNA-BINDING DOMAIN (RESIDUES 1-50) FROM TETR
REMARK 999 VARIANT B AND THE EFFECTOR-BINDING DOMAIN (RESIDUES 51-208) FROM
REMARK 999 TETR VARIANT D
DBREF 3FK6 A 1 50 UNP P04483 TETR2_ECOLX 1 50
DBREF 3FK6 A 51 208 UNP P0ACT4 TETR4_ECOLX 51 208
DBREF 3FK6 B 1 50 UNP P04483 TETR2_ECOLX 1 50
DBREF 3FK6 B 51 208 UNP P0ACT4 TETR4_ECOLX 51 208
SEQADV 3FK6 LYS A 64 UNP P0ACT4 HIS 64 ENGINEERED MUTATION
SEQADV 3FK6 LEU A 135 UNP P0ACT4 SER 135 ENGINEERED MUTATION
SEQADV 3FK6 ILE A 138 UNP P0ACT4 SER 138 ENGINEERED MUTATION
SEQADV 3FK6 LYS B 64 UNP P0ACT4 HIS 64 ENGINEERED MUTATION
SEQADV 3FK6 LEU B 135 UNP P0ACT4 SER 135 ENGINEERED MUTATION
SEQADV 3FK6 ILE B 138 UNP P0ACT4 SER 138 ENGINEERED MUTATION
SEQRES 1 A 208 MET SER ARG LEU ASP LYS SER LYS VAL ILE ASN SER ALA
SEQRES 2 A 208 LEU GLU LEU LEU ASN GLU VAL GLY ILE GLU GLY LEU THR
SEQRES 3 A 208 THR ARG LYS LEU ALA GLN LYS LEU GLY VAL GLU GLN PRO
SEQRES 4 A 208 THR LEU TYR TRP HIS VAL LYS ASN LYS ARG ALA LEU LEU
SEQRES 5 A 208 ASP ALA LEU ALA VAL GLU ILE LEU ALA ARG HIS LYS ASP
SEQRES 6 A 208 TYR SER LEU PRO ALA ALA GLY GLU SER TRP GLN SER PHE
SEQRES 7 A 208 LEU ARG ASN ASN ALA MET SER PHE ARG ARG ALA LEU LEU
SEQRES 8 A 208 ARG TYR ARG ASP GLY ALA LYS VAL HIS LEU GLY THR ARG
SEQRES 9 A 208 PRO ASP GLU LYS GLN TYR ASP THR VAL GLU THR GLN LEU
SEQRES 10 A 208 ARG PHE MET THR GLU ASN GLY PHE SER LEU ARG ASP GLY
SEQRES 11 A 208 LEU TYR ALA ILE LEU ALA VAL ILE HIS PHE THR LEU GLY
SEQRES 12 A 208 ALA VAL LEU GLU GLN GLN GLU HIS THR ALA ALA LEU THR
SEQRES 13 A 208 ASP ARG PRO ALA ALA PRO ASP GLU ASN LEU PRO PRO LEU
SEQRES 14 A 208 LEU ARG GLU ALA LEU GLN ILE MET ASP SER ASP ASP GLY
SEQRES 15 A 208 GLU GLN ALA PHE LEU HIS GLY LEU GLU SER LEU ILE ARG
SEQRES 16 A 208 GLY PHE GLU VAL GLN LEU THR ALA LEU LEU GLN ILE VAL
SEQRES 1 B 208 MET SER ARG LEU ASP LYS SER LYS VAL ILE ASN SER ALA
SEQRES 2 B 208 LEU GLU LEU LEU ASN GLU VAL GLY ILE GLU GLY LEU THR
SEQRES 3 B 208 THR ARG LYS LEU ALA GLN LYS LEU GLY VAL GLU GLN PRO
SEQRES 4 B 208 THR LEU TYR TRP HIS VAL LYS ASN LYS ARG ALA LEU LEU
SEQRES 5 B 208 ASP ALA LEU ALA VAL GLU ILE LEU ALA ARG HIS LYS ASP
SEQRES 6 B 208 TYR SER LEU PRO ALA ALA GLY GLU SER TRP GLN SER PHE
SEQRES 7 B 208 LEU ARG ASN ASN ALA MET SER PHE ARG ARG ALA LEU LEU
SEQRES 8 B 208 ARG TYR ARG ASP GLY ALA LYS VAL HIS LEU GLY THR ARG
SEQRES 9 B 208 PRO ASP GLU LYS GLN TYR ASP THR VAL GLU THR GLN LEU
SEQRES 10 B 208 ARG PHE MET THR GLU ASN GLY PHE SER LEU ARG ASP GLY
SEQRES 11 B 208 LEU TYR ALA ILE LEU ALA VAL ILE HIS PHE THR LEU GLY
SEQRES 12 B 208 ALA VAL LEU GLU GLN GLN GLU HIS THR ALA ALA LEU THR
SEQRES 13 B 208 ASP ARG PRO ALA ALA PRO ASP GLU ASN LEU PRO PRO LEU
SEQRES 14 B 208 LEU ARG GLU ALA LEU GLN ILE MET ASP SER ASP ASP GLY
SEQRES 15 B 208 GLU GLN ALA PHE LEU HIS GLY LEU GLU SER LEU ILE ARG
SEQRES 16 B 208 GLY PHE GLU VAL GLN LEU THR ALA LEU LEU GLN ILE VAL
FORMUL 3 HOH *116(H2 O)
HELIX 1 1 ASP A 5 LEU A 25 1 21
HELIX 2 2 THR A 26 GLY A 35 1 10
HELIX 3 3 GLU A 37 TRP A 43 1 7
HELIX 4 4 ASN A 47 LYS A 64 1 18
HELIX 5 5 SER A 74 ARG A 92 1 19
HELIX 6 6 ASP A 95 LEU A 101 1 7
HELIX 7 7 ASP A 106 LYS A 108 5 3
HELIX 8 8 GLN A 109 ASN A 123 1 15
HELIX 9 9 SER A 126 ALA A 154 1 29
HELIX 10 10 PRO A 167 SER A 179 1 13
HELIX 11 11 GLY A 182 GLN A 206 1 25
HELIX 12 12 ASP B 5 LEU B 25 1 21
HELIX 13 13 THR B 26 GLY B 35 1 10
HELIX 14 14 GLU B 37 TYR B 42 1 6
HELIX 15 15 ASN B 47 LYS B 64 1 18
HELIX 16 16 SER B 74 TYR B 93 1 20
HELIX 17 17 ASP B 95 LEU B 101 1 7
HELIX 18 18 ASP B 106 LYS B 108 5 3
HELIX 19 19 GLN B 109 ASN B 123 1 15
HELIX 20 20 SER B 126 LEU B 155 1 30
HELIX 21 21 PRO B 167 ASP B 178 1 12
HELIX 22 22 GLY B 182 ALA B 203 1 22
CRYST1 126.350 58.060 62.620 90.00 96.58 90.00 C 1 2 1 8
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 0.007915 0.000000 0.000913 0.00000
SCALE2 0.000000 0.017224 0.000000 0.00000
SCALE3 0.000000 0.000000 0.016075 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
