PDB Short entry for 1LBG
HEADER COMPLEX (TRANSCRIPTION REGULATION/DNA) 17-FEB-96 1LBG
TITLE LACTOSE OPERON REPRESSOR BOUND TO 21-BASE PAIR SYMMETRIC
TITLE 2 OPERATOR DNA, ALPHA CARBONS ONLY
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: LACTOSE OPERON REPRESSOR;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 ENGINEERED: YES;
COMPND 5 MOL_ID: 2;
COMPND 6 MOLECULE: 21-BASE PAIR SYMMETRIC OPERATOR DNA;
COMPND 7 CHAIN: E, F, G, H;
COMPND 8 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 STRAIN: GM1;
SOURCE 4 EXPRESSION_SYSTEM_PLASMID: PIQ;
SOURCE 5 EXPRESSION_SYSTEM_GENE: LACI;
SOURCE 6 MOL_ID: 2;
SOURCE 7 SYNTHETIC: YES
KEYWDS TRANSCRIPTION REGULATION, DNA-BINDING, REPRESSOR
EXPDTA X-RAY DIFFRACTION
AUTHOR M.LEWIS,G.CHANG,N.C.HORTON,M.A.KERCHER,H.C.PACE,P.LU
REVDAT 1 11-JUL-96 1LBG 0
JRNL AUTH M.LEWIS,G.CHANG,N.C.HORTON,M.A.KERCHER,H.C.PACE,
JRNL AUTH 2 M.A.SCHUMACHER,R.G.BRENNAN,P.LU
JRNL TITL CRYSTAL STRUCTURE OF THE LACTOSE OPERON REPRESSOR
JRNL TITL 2 AND ITS COMPLEXES WITH DNA AND INDUCER
JRNL REF SCIENCE V. 271 1247 1996
JRNL REFN ASTM SCIEAS US ISSN 0036-8075 0038
REMARK 1
REMARK 2
REMARK 2 RESOLUTION. 4.8 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.1
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 4.8
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 15.0
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.
REMARK 3 COMPLETENESS FOR RANGE (%) : NULL
REMARK 3 NUMBER OF REFLECTIONS : NULL
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) : 0.260
REMARK 3 FREE R VALUE : NULL
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : NULL
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : NULL
REMARK 3 BIN RESOLUTION RANGE LOW (A) : NULL
REMARK 3 COMPLETENESS IN THIS BIN (%) : 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 : 1428
REMARK 3 NUCLEIC ACID ATOMS : 1716
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 0
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 15.0
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
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
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.011
REMARK 3 BOND ANGLES (DEGREES) : 1.8
REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL
REMARK 3 IMPROPER ANGLES (DEGREES) : 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 NCS MODEL : NULL
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 0 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 0 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : NULL
REMARK 3 PARAMETER FILE 2 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3 TOPOLOGY FILE 2 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1LBG COMPLIES WITH FORMAT V. 2.0, 16-FEB-1996
REMARK 6
REMARK 6 THERE ARE FOUR DNA CHAINS DESIGNATED BY E, F, G, AND H.
REMARK 6 THERE ARE FOUR PROTEIN CHAINS DESIGNATED A, B, C, AND D.
REMARK 7
REMARK 7 COORDINATES FOR ONLY CARBON ALPHAS ARE GIVEN DUE TO 4.8
REMARK 7 ANGSTROM RESOLUTION.
REMARK 8
REMARK 8 GENERATED SYMMETRY MOLECULES YIELD CLOSE CONTACTS IN
REMARK 8 CRYSTAL PACKING. THIS IS PARTICULARLY TRUE FOR ATOMS OF
REMARK 8 LAC RESIDUES 351 AND 350 OF CHAIN D WHICH CONFLICT WITH END
REMARK 8 BASE G IN CHAIN G. THE ELECTRON DENSITY FOR THE ENDS OF
REMARK 8 THE DNA STRANDS IS WEAK. THE POSITION OF THE END BASE G IN
REMARK 8 DNA CHAIN G SHOULD BE USED WITH CAUTION.
REMARK 9
REMARK 9 THERE IS NO CLEAR ELECTRON DENSITY FOR THE THREE MISSING
REMARK 9 RESIDUES IN ALL FOUR CHAINS.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : NULL
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : NULL
REMARK 200 RADIATION SOURCE : NULL
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.54
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : AREA DETECTOR
REMARK 200 DETECTOR MANUFACTURER : SIEMENS
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : NULL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 11283
REMARK 200 RESOLUTION RANGE HIGH (A) : NULL
REMARK 200 RESOLUTION RANGE LOW (A) : NULL
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 90.
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : 0.058
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : NULL
REMARK 200
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 65.5
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): NULL
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
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 1/2+X,1/2+Y,Z
REMARK 290 4555 1/2-X,1/2+Y,-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 52.14852
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 112.20826
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 52.14852
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 112.20826
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. SOME OF THESE MAY BE ATOMS
REMARK 500 LOCATED ON SPECIAL POSITIONS IN THE CELL.
REMARK 500
REMARK 500 DISTANCE CUTOFF: 2.2 ANGSTROMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 N7 G G 600 CA ARG D 351 1455 0.37
REMARK 500 CA ARG D 351 N7 G G 600 1655 0.37
REMARK 500 CA ARG D 351 C5 G G 600 1655 1.24
REMARK 500 C5 G G 600 CA ARG D 351 1455 1.24
REMARK 500 CA ALA D 350 O6 G G 600 1655 1.38
REMARK 500 O6 G G 600 CA ALA D 350 1455 1.38
REMARK 500 CA ARG D 351 C8 G G 600 1655 1.46
REMARK 500 C8 G G 600 CA ARG D 351 1455 1.46
REMARK 500 C6 G G 600 CA ALA D 350 1455 2.06
REMARK 500 CA ALA D 350 C6 G G 600 1655 2.06
REMARK 500 CA ARG D 351 C4 G G 600 1655 2.18
REMARK 500 C4 G G 600 CA ARG D 351 1455 2.18
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 1LBG A SWS P03023 358 - 360 NOT IN ATOMS LIST
REMARK 999 1LBG B SWS P03023 358 - 360 NOT IN ATOMS LIST
REMARK 999 1LBG C SWS P03023 358 - 360 NOT IN ATOMS LIST
REMARK 999 1LBG D SWS P03023 358 - 360 NOT IN ATOMS LIST
REMARK 999
REMARK 999 DIFFERENT RESIDUE: THR A 109 ()
REMARK 999 SEQUENCE CORRECTED IN: J.L.BETZ, GENE, 42, 283 (1986)
REMARK 999 DIFFERENT RESIDUE: THR B 109 ()
REMARK 999 SEQUENCE CORRECTED IN: J.L.BETZ, GENE, 42, 283 (1986)
REMARK 999 DIFFERENT RESIDUE: THR C 109 ()
REMARK 999 SEQUENCE CORRECTED IN: J.L.BETZ, GENE, 42, 283 (1986)
REMARK 999 DIFFERENT RESIDUE: THR D 109 ()
REMARK 999 SEQUENCE CORRECTED IN: J.L.BETZ, GENE, 42, 283 (1986)
DBREF 1LBG A 1 357 SWS P03023 LACI_ECOLI 1 357
DBREF 1LBG B 1 357 SWS P03023 LACI_ECOLI 1 357
DBREF 1LBG C 1 357 SWS P03023 LACI_ECOLI 1 357
DBREF 1LBG D 1 357 SWS P03023 LACI_ECOLI 1 357
SEQADV 1LBG THR A 109 SWS P03023 ALA 109 CONFLICT
SEQADV 1LBG THR B 109 SWS P03023 ALA 109 CONFLICT
SEQADV 1LBG THR C 109 SWS P03023 ALA 109 CONFLICT
SEQADV 1LBG THR D 109 SWS P03023 ALA 109 CONFLICT
SEQRES 1 A 360 MET LYS PRO VAL THR LEU TYR ASP VAL ALA GLU TYR ALA
SEQRES 2 A 360 GLY VAL SER TYR GLN THR VAL SER ARG VAL VAL ASN GLN
SEQRES 3 A 360 ALA SER HIS VAL SER ALA LYS THR ARG GLU LYS VAL GLU
SEQRES 4 A 360 ALA ALA MET ALA GLU LEU ASN TYR ILE PRO ASN ARG VAL
SEQRES 5 A 360 ALA GLN GLN LEU ALA GLY LYS GLN SER LEU LEU ILE GLY
SEQRES 6 A 360 VAL ALA THR SER SER LEU ALA LEU HIS ALA PRO SER GLN
SEQRES 7 A 360 ILE VAL ALA ALA ILE LYS SER ARG ALA ASP GLN LEU GLY
SEQRES 8 A 360 ALA SER VAL VAL VAL SER MET VAL GLU ARG SER GLY VAL
SEQRES 9 A 360 GLU ALA CYS LYS THR ALA VAL HIS ASN LEU LEU ALA GLN
SEQRES 10 A 360 ARG VAL SER GLY LEU ILE ILE ASN TYR PRO LEU ASP ASP
SEQRES 11 A 360 GLN ASP ALA ILE ALA VAL GLU ALA ALA CYS THR ASN VAL
SEQRES 12 A 360 PRO ALA LEU PHE LEU ASP VAL SER ASP GLN THR PRO ILE
SEQRES 13 A 360 ASN SER ILE ILE PHE SER HIS GLU ASP GLY THR ARG LEU
SEQRES 14 A 360 GLY VAL GLU HIS LEU VAL ALA LEU GLY HIS GLN GLN ILE
SEQRES 15 A 360 ALA LEU LEU ALA GLY PRO LEU SER SER VAL SER ALA ARG
SEQRES 16 A 360 LEU ARG LEU ALA GLY TRP HIS LYS TYR LEU THR ARG ASN
SEQRES 17 A 360 GLN ILE GLN PRO ILE ALA GLU ARG GLU GLY ASP TRP SER
SEQRES 18 A 360 ALA MET SER GLY PHE GLN GLN THR MET GLN MET LEU ASN
SEQRES 19 A 360 GLU GLY ILE VAL PRO THR ALA MET LEU VAL ALA ASN ASP
SEQRES 20 A 360 GLN MET ALA LEU GLY ALA MET ARG ALA ILE THR GLU SER
SEQRES 21 A 360 GLY LEU ARG VAL GLY ALA ASP ILE SER VAL VAL GLY TYR
SEQRES 22 A 360 ASP ASP THR GLU ASP SER SER CYS TYR ILE PRO PRO LEU
SEQRES 23 A 360 THR THR ILE LYS GLN ASP PHE ARG LEU LEU GLY GLN THR
SEQRES 24 A 360 SER VAL ASP ARG LEU LEU GLN LEU SER GLN GLY GLN ALA
SEQRES 25 A 360 VAL LYS GLY ASN GLN LEU LEU PRO VAL SER LEU VAL LYS
SEQRES 26 A 360 ARG LYS THR THR LEU ALA PRO ASN THR GLN THR ALA SER
SEQRES 27 A 360 PRO ARG ALA LEU ALA ASP SER LEU MET GLN LEU ALA ARG
SEQRES 28 A 360 GLN VAL SER ARG LEU GLU SER GLY GLN
SEQRES 1 B 360 MET LYS PRO VAL THR LEU TYR ASP VAL ALA GLU TYR ALA
SEQRES 2 B 360 GLY VAL SER TYR GLN THR VAL SER ARG VAL VAL ASN GLN
SEQRES 3 B 360 ALA SER HIS VAL SER ALA LYS THR ARG GLU LYS VAL GLU
SEQRES 4 B 360 ALA ALA MET ALA GLU LEU ASN TYR ILE PRO ASN ARG VAL
SEQRES 5 B 360 ALA GLN GLN LEU ALA GLY LYS GLN SER LEU LEU ILE GLY
SEQRES 6 B 360 VAL ALA THR SER SER LEU ALA LEU HIS ALA PRO SER GLN
SEQRES 7 B 360 ILE VAL ALA ALA ILE LYS SER ARG ALA ASP GLN LEU GLY
SEQRES 8 B 360 ALA SER VAL VAL VAL SER MET VAL GLU ARG SER GLY VAL
SEQRES 9 B 360 GLU ALA CYS LYS THR ALA VAL HIS ASN LEU LEU ALA GLN
SEQRES 10 B 360 ARG VAL SER GLY LEU ILE ILE ASN TYR PRO LEU ASP ASP
SEQRES 11 B 360 GLN ASP ALA ILE ALA VAL GLU ALA ALA CYS THR ASN VAL
SEQRES 12 B 360 PRO ALA LEU PHE LEU ASP VAL SER ASP GLN THR PRO ILE
SEQRES 13 B 360 ASN SER ILE ILE PHE SER HIS GLU ASP GLY THR ARG LEU
SEQRES 14 B 360 GLY VAL GLU HIS LEU VAL ALA LEU GLY HIS GLN GLN ILE
SEQRES 15 B 360 ALA LEU LEU ALA GLY PRO LEU SER SER VAL SER ALA ARG
SEQRES 16 B 360 LEU ARG LEU ALA GLY TRP HIS LYS TYR LEU THR ARG ASN
SEQRES 17 B 360 GLN ILE GLN PRO ILE ALA GLU ARG GLU GLY ASP TRP SER
SEQRES 18 B 360 ALA MET SER GLY PHE GLN GLN THR MET GLN MET LEU ASN
SEQRES 19 B 360 GLU GLY ILE VAL PRO THR ALA MET LEU VAL ALA ASN ASP
SEQRES 20 B 360 GLN MET ALA LEU GLY ALA MET ARG ALA ILE THR GLU SER
SEQRES 21 B 360 GLY LEU ARG VAL GLY ALA ASP ILE SER VAL VAL GLY TYR
SEQRES 22 B 360 ASP ASP THR GLU ASP SER SER CYS TYR ILE PRO PRO LEU
SEQRES 23 B 360 THR THR ILE LYS GLN ASP PHE ARG LEU LEU GLY GLN THR
SEQRES 24 B 360 SER VAL ASP ARG LEU LEU GLN LEU SER GLN GLY GLN ALA
SEQRES 25 B 360 VAL LYS GLY ASN GLN LEU LEU PRO VAL SER LEU VAL LYS
SEQRES 26 B 360 ARG LYS THR THR LEU ALA PRO ASN THR GLN THR ALA SER
SEQRES 27 B 360 PRO ARG ALA LEU ALA ASP SER LEU MET GLN LEU ALA ARG
SEQRES 28 B 360 GLN VAL SER ARG LEU GLU SER GLY GLN
SEQRES 1 C 360 MET LYS PRO VAL THR LEU TYR ASP VAL ALA GLU TYR ALA
SEQRES 2 C 360 GLY VAL SER TYR GLN THR VAL SER ARG VAL VAL ASN GLN
SEQRES 3 C 360 ALA SER HIS VAL SER ALA LYS THR ARG GLU LYS VAL GLU
SEQRES 4 C 360 ALA ALA MET ALA GLU LEU ASN TYR ILE PRO ASN ARG VAL
SEQRES 5 C 360 ALA GLN GLN LEU ALA GLY LYS GLN SER LEU LEU ILE GLY
SEQRES 6 C 360 VAL ALA THR SER SER LEU ALA LEU HIS ALA PRO SER GLN
SEQRES 7 C 360 ILE VAL ALA ALA ILE LYS SER ARG ALA ASP GLN LEU GLY
SEQRES 8 C 360 ALA SER VAL VAL VAL SER MET VAL GLU ARG SER GLY VAL
SEQRES 9 C 360 GLU ALA CYS LYS THR ALA VAL HIS ASN LEU LEU ALA GLN
SEQRES 10 C 360 ARG VAL SER GLY LEU ILE ILE ASN TYR PRO LEU ASP ASP
SEQRES 11 C 360 GLN ASP ALA ILE ALA VAL GLU ALA ALA CYS THR ASN VAL
SEQRES 12 C 360 PRO ALA LEU PHE LEU ASP VAL SER ASP GLN THR PRO ILE
SEQRES 13 C 360 ASN SER ILE ILE PHE SER HIS GLU ASP GLY THR ARG LEU
SEQRES 14 C 360 GLY VAL GLU HIS LEU VAL ALA LEU GLY HIS GLN GLN ILE
SEQRES 15 C 360 ALA LEU LEU ALA GLY PRO LEU SER SER VAL SER ALA ARG
SEQRES 16 C 360 LEU ARG LEU ALA GLY TRP HIS LYS TYR LEU THR ARG ASN
SEQRES 17 C 360 GLN ILE GLN PRO ILE ALA GLU ARG GLU GLY ASP TRP SER
SEQRES 18 C 360 ALA MET SER GLY PHE GLN GLN THR MET GLN MET LEU ASN
SEQRES 19 C 360 GLU GLY ILE VAL PRO THR ALA MET LEU VAL ALA ASN ASP
SEQRES 20 C 360 GLN MET ALA LEU GLY ALA MET ARG ALA ILE THR GLU SER
SEQRES 21 C 360 GLY LEU ARG VAL GLY ALA ASP ILE SER VAL VAL GLY TYR
SEQRES 22 C 360 ASP ASP THR GLU ASP SER SER CYS TYR ILE PRO PRO LEU
SEQRES 23 C 360 THR THR ILE LYS GLN ASP PHE ARG LEU LEU GLY GLN THR
SEQRES 24 C 360 SER VAL ASP ARG LEU LEU GLN LEU SER GLN GLY GLN ALA
SEQRES 25 C 360 VAL LYS GLY ASN GLN LEU LEU PRO VAL SER LEU VAL LYS
SEQRES 26 C 360 ARG LYS THR THR LEU ALA PRO ASN THR GLN THR ALA SER
SEQRES 27 C 360 PRO ARG ALA LEU ALA ASP SER LEU MET GLN LEU ALA ARG
SEQRES 28 C 360 GLN VAL SER ARG LEU GLU SER GLY GLN
SEQRES 1 D 360 MET LYS PRO VAL THR LEU TYR ASP VAL ALA GLU TYR ALA
SEQRES 2 D 360 GLY VAL SER TYR GLN THR VAL SER ARG VAL VAL ASN GLN
SEQRES 3 D 360 ALA SER HIS VAL SER ALA LYS THR ARG GLU LYS VAL GLU
SEQRES 4 D 360 ALA ALA MET ALA GLU LEU ASN TYR ILE PRO ASN ARG VAL
SEQRES 5 D 360 ALA GLN GLN LEU ALA GLY LYS GLN SER LEU LEU ILE GLY
SEQRES 6 D 360 VAL ALA THR SER SER LEU ALA LEU HIS ALA PRO SER GLN
SEQRES 7 D 360 ILE VAL ALA ALA ILE LYS SER ARG ALA ASP GLN LEU GLY
SEQRES 8 D 360 ALA SER VAL VAL VAL SER MET VAL GLU ARG SER GLY VAL
SEQRES 9 D 360 GLU ALA CYS LYS THR ALA VAL HIS ASN LEU LEU ALA GLN
SEQRES 10 D 360 ARG VAL SER GLY LEU ILE ILE ASN TYR PRO LEU ASP ASP
SEQRES 11 D 360 GLN ASP ALA ILE ALA VAL GLU ALA ALA CYS THR ASN VAL
SEQRES 12 D 360 PRO ALA LEU PHE LEU ASP VAL SER ASP GLN THR PRO ILE
SEQRES 13 D 360 ASN SER ILE ILE PHE SER HIS GLU ASP GLY THR ARG LEU
SEQRES 14 D 360 GLY VAL GLU HIS LEU VAL ALA LEU GLY HIS GLN GLN ILE
SEQRES 15 D 360 ALA LEU LEU ALA GLY PRO LEU SER SER VAL SER ALA ARG
SEQRES 16 D 360 LEU ARG LEU ALA GLY TRP HIS LYS TYR LEU THR ARG ASN
SEQRES 17 D 360 GLN ILE GLN PRO ILE ALA GLU ARG GLU GLY ASP TRP SER
SEQRES 18 D 360 ALA MET SER GLY PHE GLN GLN THR MET GLN MET LEU ASN
SEQRES 19 D 360 GLU GLY ILE VAL PRO THR ALA MET LEU VAL ALA ASN ASP
SEQRES 20 D 360 GLN MET ALA LEU GLY ALA MET ARG ALA ILE THR GLU SER
SEQRES 21 D 360 GLY LEU ARG VAL GLY ALA ASP ILE SER VAL VAL GLY TYR
SEQRES 22 D 360 ASP ASP THR GLU ASP SER SER CYS TYR ILE PRO PRO LEU
SEQRES 23 D 360 THR THR ILE LYS GLN ASP PHE ARG LEU LEU GLY GLN THR
SEQRES 24 D 360 SER VAL ASP ARG LEU LEU GLN LEU SER GLN GLY GLN ALA
SEQRES 25 D 360 VAL LYS GLY ASN GLN LEU LEU PRO VAL SER LEU VAL LYS
SEQRES 26 D 360 ARG LYS THR THR LEU ALA PRO ASN THR GLN THR ALA SER
SEQRES 27 D 360 PRO ARG ALA LEU ALA ASP SER LEU MET GLN LEU ALA ARG
SEQRES 28 D 360 GLN VAL SER ARG LEU GLU SER GLY GLN
SEQRES 1 E 21 G A A T T G T G A G C G C
SEQRES 2 E 21 T C A C A A T T
SEQRES 1 F 21 G A A T T G T G A G C G C
SEQRES 2 F 21 T C A C A A T T
SEQRES 1 G 21 G A A T T G T G A G C G C
SEQRES 2 G 21 T C A C A A T T
SEQRES 1 H 21 G A A T T G T G A G C G C
SEQRES 2 H 21 T C A C A A T T
HELIX 1 A1 LEU A 6 TYR A 12 1
7
HELIX 2 A2 TYR A 17 ASN A 25 1
9
HELIX 3 A3 ALA A 32 LEU A 45 1
14
HELIX 4 A4 ASN A 50 GLY A 58 1
9
HELIX 5 A5 HIS A 74 LEU A 90 1
17
HELIX 6 A6 VAL A 104 ALA A 116 1
13
HELIX 7 A7 GLN A 131 GLU A 137 1
7
HELIX 8 A8 GLU A 164 VAL A 175 1
12
HELIX 9 A9 VAL A 192 LEU A 205 1
14
HELIX 10 A10 ALA A 222 LEU A 233 1
12
HELIX 11 A11 ASP A 247 GLU A 259 1
13
HELIX 12 A12 SER A 279 CYS A 281 1
3
HELIX 13 A13 PHE A 293 GLN A 309 1
17
HELIX 14 A14 ARG A 340 GLU A 357 1
18
HELIX 15 B1 LEU B 6 TYR B 12 1
7
HELIX 16 B2 TYR B 17 ASN B 25 1
9
HELIX 17 B3 ALA B 32 LEU B 45 1
14
HELIX 18 B4 ASN B 50 GLY B 58 1
9
HELIX 19 B5 HIS B 74 LEU B 90 1
17
HELIX 20 B6 VAL B 104 ALA B 116 1
13
HELIX 21 B7 GLN B 131 GLU B 137 1
7
HELIX 22 B8 GLU B 164 VAL B 175 1
12
HELIX 23 B9 VAL B 192 LEU B 205 1
14
HELIX 24 B10 ALA B 222 LEU B 233 1
12
HELIX 25 B11 ASP B 247 GLU B 259 1
13
HELIX 26 B12 SER B 279 CYS B 281 1
3
HELIX 27 B13 PHE B 293 GLN B 309 1
17
HELIX 28 B14 ARG B 340 GLU B 357 1
18
HELIX 29 C1 LEU C 6 TYR C 12 1
7
HELIX 30 C2 TYR C 17 ASN C 25 1
9
HELIX 31 C3 ALA C 32 LEU C 45 1
14
HELIX 32 C4 ASN C 50 GLY C 58 1
9
HELIX 33 C5 HIS C 74 LEU C 90 1
17
HELIX 34 C6 VAL C 104 ALA C 116 1
13
HELIX 35 C7 GLN C 131 GLU C 137 1
7
HELIX 36 C8 GLU C 164 VAL C 175 1
12
HELIX 37 C9 VAL C 192 LEU C 205 1
14
HELIX 38 C10 ALA C 222 LEU C 233 1
12
HELIX 39 C11 ASP C 247 GLU C 259 1
13
HELIX 40 C12 SER C 279 CYS C 281 1
3
HELIX 41 C13 PHE C 293 GLN C 309 1
17
HELIX 42 C14 ARG C 340 GLU C 357 1
18
HELIX 43 D1 LEU D 6 TYR D 12 1
7
HELIX 44 D2 TYR D 17 ASN D 25 1
9
HELIX 45 D3 ALA D 32 LEU D 45 1
14
HELIX 46 D4 ASN D 50 GLY D 58 1
9
HELIX 47 D5 HIS D 74 LEU D 90 1
17
HELIX 48 D6 VAL D 104 ALA D 116 1
13
HELIX 49 D7 GLN D 131 GLU D 137 1
7
HELIX 50 D8 GLU D 164 VAL D 175 1
12
HELIX 51 D9 VAL D 192 LEU D 205 1
14
HELIX 52 D10 ALA D 222 LEU D 233 1
12
HELIX 53 D11 ASP D 247 GLU D 259 1
13
HELIX 54 D12 SER D 279 CYS D 281 1
3
HELIX 55 D13 PHE D 293 GLN D 309 1
17
HELIX 56 D14 ARG D 340 GLU D 357 1
18
SHEET 1 S1A 6 ALA A 92 MET A 98 0
SHEET 2 S1A 6 LEU A 63 THR A 68 1
SHEET 3 S1A 6 GLY A 121 ILE A 124 1
SHEET 4 S1A 6 ALA A 145 ASP A 149 1
SHEET 5 S1A 6 SER A 158 PHE A 161 1
SHEET 6 S1A 6 ASN A 316 LEU A 318 1
SHEET 1 S2A 6 ALA A 214 GLU A 217 0
SHEET 2 S2A 6 ILE A 182 LEU A 185 1
SHEET 3 S2A 6 THR A 240 VAL A 244 1
SHEET 4 S2A 6 SER A 269 ASP A 274 1
SHEET 5 S2A 6 THR A 287 LYS A 290 1
SHEET 6 S2A 6 SER A 322 VAL A 324 -1
SHEET 1 S1B 6 ALA B 92 MET B 98 0
SHEET 2 S1B 6 LEU B 63 THR B 68 1
SHEET 3 S1B 6 GLY B 121 ILE B 124 1
SHEET 4 S1B 6 ALA B 145 ASP B 149 1
SHEET 5 S1B 6 SER B 158 PHE B 161 1
SHEET 6 S1B 6 ASN B 316 LEU B 318 1
SHEET 1 S2B 6 ALA B 214 GLU B 217 0
SHEET 2 S2B 6 ILE B 182 LEU B 185 1
SHEET 3 S2B 6 THR B 240 VAL B 244 1
SHEET 4 S2B 6 SER B 269 ASP B 274 1
SHEET 5 S2B 6 THR B 287 LYS B 290 1
SHEET 6 S2B 6 SER B 322 VAL B 324 -1
SHEET 1 S1C 6 ALA C 92 MET C 98 0
SHEET 2 S1C 6 LEU C 63 THR C 68 1
SHEET 3 S1C 6 GLY C 121 ILE C 124 1
SHEET 4 S1C 6 ALA C 145 ASP C 149 1
SHEET 5 S1C 6 SER C 158 PHE C 161 1
SHEET 6 S1C 6 ASN C 316 LEU C 318 1
SHEET 1 S2C 6 ALA C 214 GLU C 217 0
SHEET 2 S2C 6 ILE C 182 LEU C 185 1
SHEET 3 S2C 6 THR C 240 VAL C 244 1
SHEET 4 S2C 6 SER C 269 ASP C 274 1
SHEET 5 S2C 6 THR C 287 LYS C 290 1
SHEET 6 S2C 6 SER C 322 VAL C 324 -1
SHEET 1 S1D 6 ALA D 92 MET D 98 0
SHEET 2 S1D 6 LEU D 63 THR D 68 1
SHEET 3 S1D 6 GLY D 121 ILE D 124 1
SHEET 4 S1D 6 ALA D 145 ASP D 149 1
SHEET 5 S1D 6 SER D 158 PHE D 161 1
SHEET 6 S1D 6 ASN D 316 LEU D 318 1
SHEET 1 S2D 6 ALA D 214 GLU D 217 0
SHEET 2 S2D 6 ILE D 182 LEU D 185 1
SHEET 3 S2D 6 THR D 240 VAL D 244 1
SHEET 4 S2D 6 SER D 269 ASP D 274 1
SHEET 5 S2D 6 THR D 287 LYS D 290 1
SHEET 6 S2D 6 SER D 322 VAL D 324 -1
CRYST1 104.300 224.400 112.100 90.00 95.70 90.00 C 2 16
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 0.009588 0.000000 0.000957 0.00000
SCALE2 0.000000 0.004456 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008965 0.00000