HEADER OXIDOREDUCTASE 02-NOV-04 1WS9
TITLE CRYSTAL STRUCTURE OF PROJECT ID TT0172 FROM THERMUS THERMOPHILUS HB8
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ACYL-COA DEHYDROGENASE;
COMPND 3 CHAIN: A, B;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: THERMUS THERMOPHILUS;
SOURCE 3 ORGANISM_TAXID: 300852;
SOURCE 4 STRAIN: HB8;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET 11A
KEYWDS DEHYDROGENASE, STRUCTURAL GENOMICS, NPPSFA, NATIONAL PROJECT ON
KEYWDS 2 PROTEIN STRUCTURAL AND FUNCTIONAL ANALYSES, RIKEN STRUCTURAL
KEYWDS 3 GENOMICS/PROTEOMICS INITIATIVE, RSGI, OXIDOREDUCTASE
EXPDTA X-RAY DIFFRACTION
AUTHOR K.SHIMIZU,N.KUNISHIMA,RIKEN STRUCTURAL GENOMICS/PROTEOMICS INITIATIVE
AUTHOR 2 (RSGI)
REVDAT 4 25-OCT-23 1WS9 1 REMARK
REVDAT 3 13-JUL-11 1WS9 1 VERSN
REVDAT 2 24-FEB-09 1WS9 1 VERSN
REVDAT 1 18-OCT-05 1WS9 0
JRNL AUTH K.SHIMIZU,N.KUNISHIMA
JRNL TITL CRYSTAL STRUCTURE OF PROJECT ID TT0172 FROM THERMUS
JRNL TITL 2 THERMOPHILUS HB8
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.30 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 : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.30
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 38.71
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 3997776.380
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 34652
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) : 0.180
REMARK 3 FREE R VALUE : 0.226
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1729
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.005
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) : 2.30
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.44
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 98.60
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 5376
REMARK 3 BIN R VALUE (WORKING SET) : 0.2030
REMARK 3 BIN FREE R VALUE : 0.2460
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5.10
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 286
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.015
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 5856
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 452
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 23.60
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 38.20
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 4.08000
REMARK 3 B22 (A**2) : 4.08000
REMARK 3 B33 (A**2) : -8.16000
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) : 0.21
REMARK 3 ESD FROM SIGMAA (A) : 0.16
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) : 0.30
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.24
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.010
REMARK 3 BOND ANGLES (DEGREES) : 1.300
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 20.90
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.930
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) : 1.250 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 1.950 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 2.150 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 3.170 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.36
REMARK 3 BSOL : 55.88
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 : ION.PARAM
REMARK 3 PARAMETER FILE 4 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : WATER.TOP
REMARK 3 TOPOLOGY FILE 3 : ION.TOP
REMARK 3 TOPOLOGY FILE 4 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1WS9 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 08-NOV-04.
REMARK 100 THE DEPOSITION ID IS D_1000023939.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 09-JUL-04
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.6
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) : 1.0
REMARK 200 MONOCHROMATOR : MIRROR
REMARK 200 OPTICS : MIRROR
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : RIGAKU JUPITER
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 34652
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.300
REMARK 200 RESOLUTION RANGE LOW (A) : 40.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 5.800
REMARK 200 R MERGE (I) : 0.06800
REMARK 200 R SYM (I) : 0.06300
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 11.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.30
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.38
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 4.20
REMARK 200 R MERGE FOR SHELL (I) : 0.22600
REMARK 200 R SYM FOR SHELL (I) : 0.20200
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.700
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 1JQI
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 48.20
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.40
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 44 V/V(%) MPD, 0.1M ACETATE, 10 V/V(%)
REMARK 280 DIOXANE, PH 5.6, MICROBACH, TEMPERATURE 295K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 41
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 3555 -Y,X+1/2,Z+1/4
REMARK 290 4555 Y+1/2,-X,Z+3/4
REMARK 290 5555 X+1/2,Y+1/2,Z+1/2
REMARK 290 6555 -X,-Y,Z
REMARK 290 7555 -Y+1/2,X,Z+3/4
REMARK 290 8555 Y,-X+1/2,Z+1/4
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 61.20050
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 61.20050
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 53.05600
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 61.20050
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 26.52800
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 61.20050
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 79.58400
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 61.20050
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 61.20050
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 53.05600
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 7 0.000000 -1.000000 0.000000 61.20050
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 1.000000 79.58400
REMARK 290 SMTRY1 8 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 61.20050
REMARK 290 SMTRY3 8 0.000000 0.000000 1.000000 26.52800
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 300 REMARK: THE BIOLOGICAL ASSEMBLY IS A TETRAMER GENERATED FROM THE
REMARK 300 DIMER IN THE ASYMMETRIC UNIT.
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: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA,PQS
REMARK 350 TOTAL BURIED SURFACE AREA: 15140 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 53090 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -90.0 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 350 BIOMT1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 0.000000 -1.000000 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 MET A 1
REMARK 465 MET B 1
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 HIS A 92 CG HIS A 92 CD2 0.055
REMARK 500 TRP A 125 NE1 TRP A 125 CE2 0.099
REMARK 500 TRP A 150 NE1 TRP A 150 CE2 0.099
REMARK 500 TRP B 125 NE1 TRP B 125 CE2 0.122
REMARK 500 TRP B 150 NE1 TRP B 150 CE2 0.123
REMARK 500
REMARK 500 REMARK: NULL
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 PHE A 5 1.32 -65.50
REMARK 500 LEU A 95 -84.68 -86.48
REMARK 500 ASP A 135 59.84 -91.45
REMARK 500 GLU A 228 0.60 -66.17
REMARK 500 PHE A 318 14.87 -144.63
REMARK 500 LEU B 95 -80.68 -89.47
REMARK 500 PHE B 318 23.02 -144.24
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: TTK003000172.1 RELATED DB: TARGETDB
DBREF 1WS9 A 1 387 UNP Q5SGZ2 Q5SGZ2_THET8 1 387
DBREF 1WS9 B 1 387 UNP Q5SGZ2 Q5SGZ2_THET8 1 387
SEQRES 1 A 387 MET GLY LEU TRP PHE GLU GLU GLY ALA GLU GLU ARG GLN
SEQRES 2 A 387 VAL LEU GLY PRO PHE ARG GLU PHE LEU LYS ALA GLU VAL
SEQRES 3 A 387 ALA PRO GLY ALA ALA GLU ARG ASP ARG THR GLY ALA PHE
SEQRES 4 A 387 PRO TRP ASP LEU VAL ARG LYS LEU ALA GLU PHE GLY VAL
SEQRES 5 A 387 PHE GLY ALA LEU VAL PRO GLU ALA TYR GLY GLY ALA GLY
SEQRES 6 A 387 LEU SER THR ARG LEU PHE ALA ARG MET VAL GLU ALA ILE
SEQRES 7 A 387 ALA TYR TYR ASP GLY ALA LEU ALA LEU THR VAL ALA SER
SEQRES 8 A 387 HIS ASN SER LEU ALA THR GLY HIS ILE LEU LEU ALA GLY
SEQRES 9 A 387 SER GLU ALA GLN LYS GLU ALA PHE LEU PRO LYS LEU ALA
SEQRES 10 A 387 SER GLY GLU ALA LEU GLY ALA TRP GLY LEU THR GLU PRO
SEQRES 11 A 387 GLY SER GLY SER ASP ALA ALA ALA LEU LYS THR LYS ALA
SEQRES 12 A 387 GLU LYS VAL GLU GLY GLY TRP ARG LEU ASN GLY THR LYS
SEQRES 13 A 387 GLN PHE ILE THR GLN GLY SER VAL ALA GLY VAL TYR VAL
SEQRES 14 A 387 VAL MET ALA ARG THR ASP PRO PRO PRO SER PRO GLU ARG
SEQRES 15 A 387 LYS HIS GLN GLY ILE SER ALA PHE ALA PHE PHE ARG PRO
SEQRES 16 A 387 GLU ARG GLY LEU LYS VAL GLY ARG LYS GLU GLU LYS LEU
SEQRES 17 A 387 GLY LEU THR ALA SER ASP THR ALA GLN LEU ILE LEU GLU
SEQRES 18 A 387 ASP LEU PHE VAL PRO GLU GLU ALA LEU LEU GLY GLU ARG
SEQRES 19 A 387 GLY LYS GLY PHE TYR ASP VAL LEU ARG VAL LEU ASP GLY
SEQRES 20 A 387 GLY ARG ILE GLY ILE ALA ALA MET ALA VAL GLY LEU GLY
SEQRES 21 A 387 GLN ALA ALA LEU ASP TYR ALA LEU ALA TYR ALA LYS GLY
SEQRES 22 A 387 ARG GLU ALA PHE GLY ARG PRO ILE ALA GLU PHE GLU GLY
SEQRES 23 A 387 VAL SER PHE LYS LEU ALA GLU ALA ALA THR GLU LEU GLU
SEQRES 24 A 387 ALA ALA ARG LEU LEU TYR LEU LYS ALA ALA GLU LEU LYS
SEQRES 25 A 387 ASP ALA GLY ARG PRO PHE THR LEU GLU ALA ALA GLN ALA
SEQRES 26 A 387 LYS LEU PHE ALA SER GLU ALA ALA VAL LYS ALA CYS ASP
SEQRES 27 A 387 GLU ALA ILE GLN ILE LEU GLY GLY TYR GLY TYR VAL LYS
SEQRES 28 A 387 ASP TYR PRO VAL GLU ARG TYR TRP ARG ASP ALA ARG LEU
SEQRES 29 A 387 THR ARG ILE GLY GLU GLY THR SER GLU ILE LEU LYS LEU
SEQRES 30 A 387 VAL ILE ALA ARG ARG LEU LEU GLU ALA VAL
SEQRES 1 B 387 MET GLY LEU TRP PHE GLU GLU GLY ALA GLU GLU ARG GLN
SEQRES 2 B 387 VAL LEU GLY PRO PHE ARG GLU PHE LEU LYS ALA GLU VAL
SEQRES 3 B 387 ALA PRO GLY ALA ALA GLU ARG ASP ARG THR GLY ALA PHE
SEQRES 4 B 387 PRO TRP ASP LEU VAL ARG LYS LEU ALA GLU PHE GLY VAL
SEQRES 5 B 387 PHE GLY ALA LEU VAL PRO GLU ALA TYR GLY GLY ALA GLY
SEQRES 6 B 387 LEU SER THR ARG LEU PHE ALA ARG MET VAL GLU ALA ILE
SEQRES 7 B 387 ALA TYR TYR ASP GLY ALA LEU ALA LEU THR VAL ALA SER
SEQRES 8 B 387 HIS ASN SER LEU ALA THR GLY HIS ILE LEU LEU ALA GLY
SEQRES 9 B 387 SER GLU ALA GLN LYS GLU ALA PHE LEU PRO LYS LEU ALA
SEQRES 10 B 387 SER GLY GLU ALA LEU GLY ALA TRP GLY LEU THR GLU PRO
SEQRES 11 B 387 GLY SER GLY SER ASP ALA ALA ALA LEU LYS THR LYS ALA
SEQRES 12 B 387 GLU LYS VAL GLU GLY GLY TRP ARG LEU ASN GLY THR LYS
SEQRES 13 B 387 GLN PHE ILE THR GLN GLY SER VAL ALA GLY VAL TYR VAL
SEQRES 14 B 387 VAL MET ALA ARG THR ASP PRO PRO PRO SER PRO GLU ARG
SEQRES 15 B 387 LYS HIS GLN GLY ILE SER ALA PHE ALA PHE PHE ARG PRO
SEQRES 16 B 387 GLU ARG GLY LEU LYS VAL GLY ARG LYS GLU GLU LYS LEU
SEQRES 17 B 387 GLY LEU THR ALA SER ASP THR ALA GLN LEU ILE LEU GLU
SEQRES 18 B 387 ASP LEU PHE VAL PRO GLU GLU ALA LEU LEU GLY GLU ARG
SEQRES 19 B 387 GLY LYS GLY PHE TYR ASP VAL LEU ARG VAL LEU ASP GLY
SEQRES 20 B 387 GLY ARG ILE GLY ILE ALA ALA MET ALA VAL GLY LEU GLY
SEQRES 21 B 387 GLN ALA ALA LEU ASP TYR ALA LEU ALA TYR ALA LYS GLY
SEQRES 22 B 387 ARG GLU ALA PHE GLY ARG PRO ILE ALA GLU PHE GLU GLY
SEQRES 23 B 387 VAL SER PHE LYS LEU ALA GLU ALA ALA THR GLU LEU GLU
SEQRES 24 B 387 ALA ALA ARG LEU LEU TYR LEU LYS ALA ALA GLU LEU LYS
SEQRES 25 B 387 ASP ALA GLY ARG PRO PHE THR LEU GLU ALA ALA GLN ALA
SEQRES 26 B 387 LYS LEU PHE ALA SER GLU ALA ALA VAL LYS ALA CYS ASP
SEQRES 27 B 387 GLU ALA ILE GLN ILE LEU GLY GLY TYR GLY TYR VAL LYS
SEQRES 28 B 387 ASP TYR PRO VAL GLU ARG TYR TRP ARG ASP ALA ARG LEU
SEQRES 29 B 387 THR ARG ILE GLY GLU GLY THR SER GLU ILE LEU LYS LEU
SEQRES 30 B 387 VAL ILE ALA ARG ARG LEU LEU GLU ALA VAL
FORMUL 3 HOH *452(H2 O)
HELIX 1 1 GLY A 8 VAL A 26 1 19
HELIX 2 2 GLY A 29 GLY A 37 1 9
HELIX 3 3 PRO A 40 GLU A 49 1 10
HELIX 4 4 PHE A 50 ALA A 55 5 6
HELIX 5 5 PRO A 58 GLY A 62 5 5
HELIX 6 6 SER A 67 ASP A 82 1 16
HELIX 7 7 ASP A 82 LEU A 95 1 14
HELIX 8 8 LEU A 95 GLY A 104 1 10
HELIX 9 9 SER A 105 SER A 118 1 14
HELIX 10 10 ASP A 135 LEU A 139 5 5
HELIX 11 11 SER A 179 LYS A 183 5 5
HELIX 12 12 LYS A 236 ARG A 274 1 39
HELIX 13 13 PRO A 280 GLU A 283 5 4
HELIX 14 14 PHE A 284 ALA A 314 1 31
HELIX 15 15 PHE A 318 GLY A 345 1 28
HELIX 16 16 GLY A 346 VAL A 350 5 5
HELIX 17 17 PRO A 354 ARG A 363 1 10
HELIX 18 18 LEU A 364 ILE A 367 5 4
HELIX 19 19 THR A 371 ALA A 386 1 16
HELIX 20 20 GLY B 8 VAL B 26 1 19
HELIX 21 21 GLY B 29 GLY B 37 1 9
HELIX 22 22 PRO B 40 PHE B 50 1 11
HELIX 23 23 PRO B 58 GLY B 62 5 5
HELIX 24 24 SER B 67 ASP B 82 1 16
HELIX 25 25 ASP B 82 LEU B 95 1 14
HELIX 26 26 LEU B 95 GLY B 104 1 10
HELIX 27 27 SER B 105 SER B 118 1 14
HELIX 28 28 ASP B 135 LEU B 139 5 5
HELIX 29 29 SER B 179 LYS B 183 5 5
HELIX 30 30 LYS B 236 ARG B 274 1 39
HELIX 31 31 PHE B 284 ALA B 314 1 31
HELIX 32 32 PHE B 318 LEU B 344 1 27
HELIX 33 33 GLY B 345 VAL B 350 5 6
HELIX 34 34 PRO B 354 ARG B 363 1 10
HELIX 35 35 LEU B 364 ILE B 367 5 4
HELIX 36 36 THR B 371 ALA B 386 1 16
SHEET 1 A 4 GLY A 123 GLY A 126 0
SHEET 2 A 4 VAL A 167 ARG A 173 1 O VAL A 169 N GLY A 126
SHEET 3 A 4 ILE A 187 PHE A 193 -1 O PHE A 192 N TYR A 168
SHEET 4 A 4 LEU A 230 LEU A 231 -1 O LEU A 231 N ALA A 189
SHEET 1 B 4 LYS A 142 VAL A 146 0
SHEET 2 B 4 GLY A 149 THR A 160 -1 O GLY A 149 N VAL A 146
SHEET 3 B 4 THR A 215 PRO A 226 -1 O LEU A 220 N GLY A 154
SHEET 4 B 4 LEU A 199 VAL A 201 -1 N LYS A 200 O ILE A 219
SHEET 1 C 4 GLY B 123 GLY B 126 0
SHEET 2 C 4 VAL B 167 ARG B 173 1 O VAL B 169 N GLY B 126
SHEET 3 C 4 ILE B 187 PHE B 193 -1 O PHE B 192 N TYR B 168
SHEET 4 C 4 LEU B 230 LEU B 231 -1 O LEU B 231 N ALA B 189
SHEET 1 D 4 LYS B 142 VAL B 146 0
SHEET 2 D 4 GLY B 149 THR B 160 -1 O ARG B 151 N GLU B 144
SHEET 3 D 4 THR B 215 PRO B 226 -1 O LEU B 223 N LEU B 152
SHEET 4 D 4 LEU B 199 VAL B 201 -1 N LYS B 200 O ILE B 219
SHEET 1 E 2 GLU B 275 ALA B 276 0
SHEET 2 E 2 ARG B 279 PRO B 280 -1 O ARG B 279 N ALA B 276
CRYST1 122.401 122.401 106.112 90.00 90.00 90.00 I 41 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 0.008170 0.000000 0.000000 0.00000
SCALE2 0.000000 0.008170 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009424 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
