HEADER TRANSFERASE 27-APR-07 2YXZ
TITLE CRYSTAL STRUCTURE OF TT0281 FROM THERMUS THERMOPHILUS HB8
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: THIAMIN-MONOPHOSPHATE KINASE;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 EC: 2.7.4.16;
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 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: ROSETTA-GAMITM(DE3);
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET-11A
KEYWDS ALPHA/BETA STRUCTURE, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR M.GOTO
REVDAT 4 13-MAR-24 2YXZ 1 REMARK
REVDAT 3 13-JUL-11 2YXZ 1 VERSN
REVDAT 2 24-FEB-09 2YXZ 1 VERSN
REVDAT 1 29-APR-08 2YXZ 0
JRNL AUTH T.MATSUSHITA,M.KAN,M.GOTO,I.MIYAHARA,N.KAMIYA
JRNL TITL CRYSTAL STRUCTURE OF TT0281 FROM THERMUS THERMOPHILUS HB8
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.90 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) : 1.90
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 48.65
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 2328165.930
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 92.4
REMARK 3 NUMBER OF REFLECTIONS : 91864
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) : 0.225
REMARK 3 FREE R VALUE : 0.264
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 10.000
REMARK 3 FREE R VALUE TEST SET COUNT : 9188
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.003
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) : 1.90
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.02
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 79.50
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 11782
REMARK 3 BIN R VALUE (WORKING SET) : 0.2990
REMARK 3 BIN FREE R VALUE : 0.3350
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 10.10
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 1322
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.009
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 8836
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 418
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 18.70
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 35.70
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 10.40000
REMARK 3 B22 (A**2) : -0.37000
REMARK 3 B33 (A**2) : -10.03000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -7.79000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.25
REMARK 3 ESD FROM SIGMAA (A) : 0.26
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) : 0.29
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.005
REMARK 3 BOND ANGLES (DEGREES) : 1.300
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 23.20
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.800
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) : 1.210 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 1.780 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 1.860 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 2.720 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.38
REMARK 3 BSOL : 59.55
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 : WAT.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 2YXZ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 01-MAY-07.
REMARK 100 THE DEPOSITION ID IS D_1000027275.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 04-JUL-05
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SPRING-8
REMARK 200 BEAMLINE : BL41XU
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 : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 91864
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.900
REMARK 200 RESOLUTION RANGE LOW (A) : 171.499
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 92.2
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
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) : 1.90
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.97
REMARK 200 COMPLETENESS FOR SHELL (%) : 76.7
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 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MIR
REMARK 200 SOFTWARE USED: SHARP
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 48.89
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.41
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: AMMONIUM SULFATE, DIOXANE, HEPES-NA,
REMARK 280 PH 7.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K
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 70.78200
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 26.09500
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 70.78200
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 26.09500
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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: 5390 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 22890 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -38.1 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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
REMARK 350 BIOMOLECULE: 2
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: 4970 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 22500 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -41.6 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, D
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 LYS A 306
REMARK 465 GLY A 307
REMARK 465 TYR A 308
REMARK 465 ALA A 309
REMARK 465 HIS A 310
REMARK 465 PHE A 311
REMARK 465 LYS B 306
REMARK 465 GLY B 307
REMARK 465 TYR B 308
REMARK 465 ALA B 309
REMARK 465 HIS B 310
REMARK 465 PHE B 311
REMARK 465 LYS C 306
REMARK 465 GLY C 307
REMARK 465 TYR C 308
REMARK 465 ALA C 309
REMARK 465 HIS C 310
REMARK 465 PHE C 311
REMARK 465 MET D 1
REMARK 465 LYS D 306
REMARK 465 GLY D 307
REMARK 465 TYR D 308
REMARK 465 ALA D 309
REMARK 465 HIS D 310
REMARK 465 PHE D 311
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 9 CG CD NE CZ NH1 NH2
REMARK 470 ARG A 14 CG CD NE CZ NH1 NH2
REMARK 470 GLU A 23 CG CD OE1 OE2
REMARK 470 LYS A 57 CG CD CE NZ
REMARK 470 GLU A 94 CG CD OE1 OE2
REMARK 470 ARG A 126 CG CD NE CZ NH1 NH2
REMARK 470 GLU A 141 CG CD OE1 OE2
REMARK 470 TYR A 172 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 GLU A 230 CG CD OE1 OE2
REMARK 470 GLU A 246 CG CD OE1 OE2
REMARK 470 GLU A 268 CG CD OE1 OE2
REMARK 470 ARG A 289 CG CD NE CZ NH1 NH2
REMARK 470 LEU B 6 CG CD1 CD2
REMARK 470 ARG B 9 CG CD NE CZ NH1 NH2
REMARK 470 GLU B 23 CG CD OE1 OE2
REMARK 470 GLU B 38 CG CD OE1 OE2
REMARK 470 ARG B 52 CG CD NE CZ NH1 NH2
REMARK 470 LYS B 57 CG CD CE NZ
REMARK 470 GLU B 94 CG CD OE1 OE2
REMARK 470 GLU B 97 CG CD OE1 OE2
REMARK 470 GLU B 98 CG CD OE1 OE2
REMARK 470 ARG B 114 CG CD NE CZ NH1 NH2
REMARK 470 ARG B 126 CG CD NE CZ NH1 NH2
REMARK 470 GLU B 129 CG CD OE1 OE2
REMARK 470 LYS B 147 CG CD CE NZ
REMARK 470 LEU B 191 CG CD1 CD2
REMARK 470 GLU B 246 CG CD OE1 OE2
REMARK 470 GLU B 250 CG CD OE1 OE2
REMARK 470 GLN B 267 CG CD OE1 NE2
REMARK 470 GLU B 268 CG CD OE1 OE2
REMARK 470 LYS B 278 CG CD CE NZ
REMARK 470 GLU B 294 CG CD OE1 OE2
REMARK 470 LYS C 4 CG CD CE NZ
REMARK 470 GLU C 8 CG CD OE1 OE2
REMARK 470 ARG C 14 CG CD NE CZ NH1 NH2
REMARK 470 LYS C 57 CG CD CE NZ
REMARK 470 ARG C 126 CG CD NE CZ NH1 NH2
REMARK 470 GLU C 246 CG CD OE1 OE2
REMARK 470 LYS C 278 CG CD CE NZ
REMARK 470 ARG D 2 CG CD NE CZ NH1 NH2
REMARK 470 LYS D 4 CG CD CE NZ
REMARK 470 GLU D 8 CG CD OE1 OE2
REMARK 470 ARG D 9 CG CD NE CZ NH1 NH2
REMARK 470 LEU D 12 CG CD1 CD2
REMARK 470 ARG D 14 CG CD NE CZ NH1 NH2
REMARK 470 LEU D 18 CG CD1 CD2
REMARK 470 GLU D 23 CG CD OE1 OE2
REMARK 470 ARG D 40 CG CD NE CZ NH1 NH2
REMARK 470 LYS D 57 CG CD CE NZ
REMARK 470 GLU D 94 CG CD OE1 OE2
REMARK 470 ARG D 106 CG CD NE CZ NH1 NH2
REMARK 470 ARG D 126 CG CD NE CZ NH1 NH2
REMARK 470 LEU D 139 CG CD1 CD2
REMARK 470 LYS D 182 CG CD CE NZ
REMARK 470 GLU D 230 CG CD OE1 OE2
REMARK 470 GLU D 246 CG CD OE1 OE2
REMARK 470 LYS D 278 CG CD CE NZ
REMARK 470 LYS D 280 CG CD CE NZ
REMARK 470 ARG D 289 CG CD NE CZ NH1 NH2
REMARK 470 GLU D 294 CG CD OE1 OE2
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 GLU A 23 63.37 -112.93
REMARK 500 PRO A 190 97.23 -64.41
REMARK 500 PRO B 190 79.50 -68.64
REMARK 500 ASP B 222 -8.91 -59.24
REMARK 500 ARG B 299 55.23 36.98
REMARK 500 PRO C 190 93.76 -61.86
REMARK 500 LYS D 4 -7.40 -53.44
REMARK 500 ALA D 117 -169.21 -115.99
REMARK 500
REMARK 500 REMARK: NULL
DBREF 2YXZ A 1 311 UNP Q5SL69 Q5SL69_THET8 1 311
DBREF 2YXZ B 1 311 UNP Q5SL69 Q5SL69_THET8 1 311
DBREF 2YXZ C 1 311 UNP Q5SL69 Q5SL69_THET8 1 311
DBREF 2YXZ D 1 311 UNP Q5SL69 Q5SL69_THET8 1 311
SEQRES 1 A 311 MET ARG LEU LYS ASP LEU GLY GLU ARG ALA LEU LEU ALA
SEQRES 2 A 311 ARG LEU ALA PRO LEU GLY TYR PRO PRO GLU ALA PRO LEU
SEQRES 3 A 311 PRO PRO GLY ASP ASP ALA GLY GLY VAL TRP ALA GLU GLY
SEQRES 4 A 311 ARG ALA TRP LEU LEU LYS THR ASP GLY PHE LEU TYR ARG
SEQRES 5 A 311 GLU VAL ALA LEU LYS GLY MET GLY PRO PHE GLU VAL GLY
SEQRES 6 A 311 PHE ARG GLY VAL ALA ALA THR ALA SER ASP LEU LEU ALA
SEQRES 7 A 311 LYS MET GLY ARG PRO LEU GLY PHE THR LEU GLY LEU PHE
SEQRES 8 A 311 LEU PRO GLU ASP LEU GLU GLU GLY PHE VAL LEU GLU LEU
SEQRES 9 A 311 VAL ARG GLY ALA ALA GLU ALA ALA LYS ARG LEU GLY ALA
SEQRES 10 A 311 PHE LEU LEU GLY GLY ASP THR ASN ARG GLY VAL GLU VAL
SEQRES 11 A 311 ALA LEU THR VAL SER GLY TYR ALA LEU ALA GLU ALA PRO
SEQRES 12 A 311 LEU PRO ARG LYS ALA LEU PRO GLY ASP LEU LEU TYR LEU
SEQRES 13 A 311 ALA GLY ASP ARG TRP GLY ARG THR GLY ALA ALA ILE ARG
SEQRES 14 A 311 ALA HIS TYR GLU GLY ARG SER LEU GLU GLY PHE PRO LYS
SEQRES 15 A 311 ILE ARG GLU ALA ALA PHE TYR PRO LEU PRO ARG LEU GLU
SEQRES 16 A 311 LEU LEU ALA LEU SER GLY LEU LEU ARG GLY SER LEU ASP
SEQRES 17 A 311 SER SER ASP GLY LEU ALA GLU THR LEU TRP GLN LEU ALA
SEQRES 18 A 311 ASP LEU GLY VAL GLY VAL GLU VAL GLU ALA LEU PRO LEU
SEQRES 19 A 311 TYR PRO ASP VAL LEU ALA PHE ALA GLY SER GLU GLU ALA
SEQRES 20 A 311 ALA LEU GLU LEU VAL LEU TYR GLY GLY GLU GLU PHE GLU
SEQRES 21 A 311 ALA VAL LEU VAL VAL PRO GLN GLU GLY ALA ALA ALA VAL
SEQRES 22 A 311 GLU ALA ARG ALA LYS ALA LYS GLY LEU PRO LEU PHE ARG
SEQRES 23 A 311 ALA GLY ARG VAL VAL ALA GLY GLU GLY VAL TYR LEU ARG
SEQRES 24 A 311 GLY ALA PRO LEU PRO ARG LYS GLY TYR ALA HIS PHE
SEQRES 1 B 311 MET ARG LEU LYS ASP LEU GLY GLU ARG ALA LEU LEU ALA
SEQRES 2 B 311 ARG LEU ALA PRO LEU GLY TYR PRO PRO GLU ALA PRO LEU
SEQRES 3 B 311 PRO PRO GLY ASP ASP ALA GLY GLY VAL TRP ALA GLU GLY
SEQRES 4 B 311 ARG ALA TRP LEU LEU LYS THR ASP GLY PHE LEU TYR ARG
SEQRES 5 B 311 GLU VAL ALA LEU LYS GLY MET GLY PRO PHE GLU VAL GLY
SEQRES 6 B 311 PHE ARG GLY VAL ALA ALA THR ALA SER ASP LEU LEU ALA
SEQRES 7 B 311 LYS MET GLY ARG PRO LEU GLY PHE THR LEU GLY LEU PHE
SEQRES 8 B 311 LEU PRO GLU ASP LEU GLU GLU GLY PHE VAL LEU GLU LEU
SEQRES 9 B 311 VAL ARG GLY ALA ALA GLU ALA ALA LYS ARG LEU GLY ALA
SEQRES 10 B 311 PHE LEU LEU GLY GLY ASP THR ASN ARG GLY VAL GLU VAL
SEQRES 11 B 311 ALA LEU THR VAL SER GLY TYR ALA LEU ALA GLU ALA PRO
SEQRES 12 B 311 LEU PRO ARG LYS ALA LEU PRO GLY ASP LEU LEU TYR LEU
SEQRES 13 B 311 ALA GLY ASP ARG TRP GLY ARG THR GLY ALA ALA ILE ARG
SEQRES 14 B 311 ALA HIS TYR GLU GLY ARG SER LEU GLU GLY PHE PRO LYS
SEQRES 15 B 311 ILE ARG GLU ALA ALA PHE TYR PRO LEU PRO ARG LEU GLU
SEQRES 16 B 311 LEU LEU ALA LEU SER GLY LEU LEU ARG GLY SER LEU ASP
SEQRES 17 B 311 SER SER ASP GLY LEU ALA GLU THR LEU TRP GLN LEU ALA
SEQRES 18 B 311 ASP LEU GLY VAL GLY VAL GLU VAL GLU ALA LEU PRO LEU
SEQRES 19 B 311 TYR PRO ASP VAL LEU ALA PHE ALA GLY SER GLU GLU ALA
SEQRES 20 B 311 ALA LEU GLU LEU VAL LEU TYR GLY GLY GLU GLU PHE GLU
SEQRES 21 B 311 ALA VAL LEU VAL VAL PRO GLN GLU GLY ALA ALA ALA VAL
SEQRES 22 B 311 GLU ALA ARG ALA LYS ALA LYS GLY LEU PRO LEU PHE ARG
SEQRES 23 B 311 ALA GLY ARG VAL VAL ALA GLY GLU GLY VAL TYR LEU ARG
SEQRES 24 B 311 GLY ALA PRO LEU PRO ARG LYS GLY TYR ALA HIS PHE
SEQRES 1 C 311 MET ARG LEU LYS ASP LEU GLY GLU ARG ALA LEU LEU ALA
SEQRES 2 C 311 ARG LEU ALA PRO LEU GLY TYR PRO PRO GLU ALA PRO LEU
SEQRES 3 C 311 PRO PRO GLY ASP ASP ALA GLY GLY VAL TRP ALA GLU GLY
SEQRES 4 C 311 ARG ALA TRP LEU LEU LYS THR ASP GLY PHE LEU TYR ARG
SEQRES 5 C 311 GLU VAL ALA LEU LYS GLY MET GLY PRO PHE GLU VAL GLY
SEQRES 6 C 311 PHE ARG GLY VAL ALA ALA THR ALA SER ASP LEU LEU ALA
SEQRES 7 C 311 LYS MET GLY ARG PRO LEU GLY PHE THR LEU GLY LEU PHE
SEQRES 8 C 311 LEU PRO GLU ASP LEU GLU GLU GLY PHE VAL LEU GLU LEU
SEQRES 9 C 311 VAL ARG GLY ALA ALA GLU ALA ALA LYS ARG LEU GLY ALA
SEQRES 10 C 311 PHE LEU LEU GLY GLY ASP THR ASN ARG GLY VAL GLU VAL
SEQRES 11 C 311 ALA LEU THR VAL SER GLY TYR ALA LEU ALA GLU ALA PRO
SEQRES 12 C 311 LEU PRO ARG LYS ALA LEU PRO GLY ASP LEU LEU TYR LEU
SEQRES 13 C 311 ALA GLY ASP ARG TRP GLY ARG THR GLY ALA ALA ILE ARG
SEQRES 14 C 311 ALA HIS TYR GLU GLY ARG SER LEU GLU GLY PHE PRO LYS
SEQRES 15 C 311 ILE ARG GLU ALA ALA PHE TYR PRO LEU PRO ARG LEU GLU
SEQRES 16 C 311 LEU LEU ALA LEU SER GLY LEU LEU ARG GLY SER LEU ASP
SEQRES 17 C 311 SER SER ASP GLY LEU ALA GLU THR LEU TRP GLN LEU ALA
SEQRES 18 C 311 ASP LEU GLY VAL GLY VAL GLU VAL GLU ALA LEU PRO LEU
SEQRES 19 C 311 TYR PRO ASP VAL LEU ALA PHE ALA GLY SER GLU GLU ALA
SEQRES 20 C 311 ALA LEU GLU LEU VAL LEU TYR GLY GLY GLU GLU PHE GLU
SEQRES 21 C 311 ALA VAL LEU VAL VAL PRO GLN GLU GLY ALA ALA ALA VAL
SEQRES 22 C 311 GLU ALA ARG ALA LYS ALA LYS GLY LEU PRO LEU PHE ARG
SEQRES 23 C 311 ALA GLY ARG VAL VAL ALA GLY GLU GLY VAL TYR LEU ARG
SEQRES 24 C 311 GLY ALA PRO LEU PRO ARG LYS GLY TYR ALA HIS PHE
SEQRES 1 D 311 MET ARG LEU LYS ASP LEU GLY GLU ARG ALA LEU LEU ALA
SEQRES 2 D 311 ARG LEU ALA PRO LEU GLY TYR PRO PRO GLU ALA PRO LEU
SEQRES 3 D 311 PRO PRO GLY ASP ASP ALA GLY GLY VAL TRP ALA GLU GLY
SEQRES 4 D 311 ARG ALA TRP LEU LEU LYS THR ASP GLY PHE LEU TYR ARG
SEQRES 5 D 311 GLU VAL ALA LEU LYS GLY MET GLY PRO PHE GLU VAL GLY
SEQRES 6 D 311 PHE ARG GLY VAL ALA ALA THR ALA SER ASP LEU LEU ALA
SEQRES 7 D 311 LYS MET GLY ARG PRO LEU GLY PHE THR LEU GLY LEU PHE
SEQRES 8 D 311 LEU PRO GLU ASP LEU GLU GLU GLY PHE VAL LEU GLU LEU
SEQRES 9 D 311 VAL ARG GLY ALA ALA GLU ALA ALA LYS ARG LEU GLY ALA
SEQRES 10 D 311 PHE LEU LEU GLY GLY ASP THR ASN ARG GLY VAL GLU VAL
SEQRES 11 D 311 ALA LEU THR VAL SER GLY TYR ALA LEU ALA GLU ALA PRO
SEQRES 12 D 311 LEU PRO ARG LYS ALA LEU PRO GLY ASP LEU LEU TYR LEU
SEQRES 13 D 311 ALA GLY ASP ARG TRP GLY ARG THR GLY ALA ALA ILE ARG
SEQRES 14 D 311 ALA HIS TYR GLU GLY ARG SER LEU GLU GLY PHE PRO LYS
SEQRES 15 D 311 ILE ARG GLU ALA ALA PHE TYR PRO LEU PRO ARG LEU GLU
SEQRES 16 D 311 LEU LEU ALA LEU SER GLY LEU LEU ARG GLY SER LEU ASP
SEQRES 17 D 311 SER SER ASP GLY LEU ALA GLU THR LEU TRP GLN LEU ALA
SEQRES 18 D 311 ASP LEU GLY VAL GLY VAL GLU VAL GLU ALA LEU PRO LEU
SEQRES 19 D 311 TYR PRO ASP VAL LEU ALA PHE ALA GLY SER GLU GLU ALA
SEQRES 20 D 311 ALA LEU GLU LEU VAL LEU TYR GLY GLY GLU GLU PHE GLU
SEQRES 21 D 311 ALA VAL LEU VAL VAL PRO GLN GLU GLY ALA ALA ALA VAL
SEQRES 22 D 311 GLU ALA ARG ALA LYS ALA LYS GLY LEU PRO LEU PHE ARG
SEQRES 23 D 311 ALA GLY ARG VAL VAL ALA GLY GLU GLY VAL TYR LEU ARG
SEQRES 24 D 311 GLY ALA PRO LEU PRO ARG LYS GLY TYR ALA HIS PHE
FORMUL 5 HOH *418(H2 O)
HELIX 1 1 ARG A 2 GLY A 7 1 6
HELIX 2 2 GLY A 7 ALA A 16 1 10
HELIX 3 3 TYR A 51 ALA A 55 1 5
HELIX 4 4 GLY A 60 LYS A 79 1 20
HELIX 5 5 GLU A 97 LEU A 115 1 19
HELIX 6 6 GLY A 162 GLY A 174 1 13
HELIX 7 7 PHE A 180 TYR A 189 1 10
HELIX 8 8 ARG A 193 SER A 200 5 8
HELIX 9 9 GLY A 212 ASP A 222 1 11
HELIX 10 10 TYR A 235 GLY A 243 1 9
HELIX 11 11 SER A 244 TYR A 254 1 11
HELIX 12 12 GLY A 269 LYS A 280 1 12
HELIX 13 13 ARG B 2 GLY B 7 1 6
HELIX 14 14 GLY B 7 ALA B 16 1 10
HELIX 15 15 TYR B 51 ALA B 55 1 5
HELIX 16 16 GLY B 60 LYS B 79 1 20
HELIX 17 17 GLU B 97 LEU B 115 1 19
HELIX 18 18 GLY B 162 GLY B 174 1 13
HELIX 19 19 PHE B 180 TYR B 189 1 10
HELIX 20 20 ARG B 193 SER B 200 5 8
HELIX 21 21 GLY B 212 ASP B 222 1 11
HELIX 22 22 TYR B 235 GLY B 243 1 9
HELIX 23 23 SER B 244 TYR B 254 1 11
HELIX 24 24 PRO B 266 LYS B 280 1 15
HELIX 25 25 ARG C 2 GLY C 7 1 6
HELIX 26 26 GLY C 7 ALA C 16 1 10
HELIX 27 27 TYR C 51 ALA C 55 1 5
HELIX 28 28 GLY C 60 LYS C 79 1 20
HELIX 29 29 GLU C 97 LEU C 115 1 19
HELIX 30 30 GLY C 162 GLY C 174 1 13
HELIX 31 31 PHE C 180 TYR C 189 1 10
HELIX 32 32 ARG C 193 SER C 200 5 8
HELIX 33 33 GLY C 212 ASP C 222 1 11
HELIX 34 34 TYR C 235 GLY C 243 1 9
HELIX 35 35 SER C 244 TYR C 254 1 11
HELIX 36 36 PRO C 266 GLU C 268 5 3
HELIX 37 37 GLY C 269 GLY C 281 1 13
HELIX 38 38 ARG D 2 GLY D 7 1 6
HELIX 39 39 GLY D 7 ALA D 16 1 10
HELIX 40 40 TYR D 51 ALA D 55 1 5
HELIX 41 41 GLY D 60 LYS D 79 1 20
HELIX 42 42 GLU D 97 LEU D 115 1 19
HELIX 43 43 GLY D 162 GLY D 174 1 13
HELIX 44 44 PHE D 180 TYR D 189 1 10
HELIX 45 45 ARG D 193 SER D 200 5 8
HELIX 46 46 GLY D 212 ASP D 222 1 11
HELIX 47 47 TYR D 235 GLY D 243 1 9
HELIX 48 48 SER D 244 TYR D 254 1 11
HELIX 49 49 GLU D 268 GLY D 281 1 14
SHEET 1 A 5 GLY A 33 ALA A 37 0
SHEET 2 A 5 ARG A 40 LEU A 50 -1 O ARG A 40 N ALA A 37
SHEET 3 A 5 ALA A 131 ALA A 140 -1 O VAL A 134 N ASP A 47
SHEET 4 A 5 GLY A 81 LEU A 92 -1 N LEU A 84 O TYR A 137
SHEET 5 A 5 PHE A 118 ARG A 126 1 O LEU A 120 N PHE A 86
SHEET 1 B 7 GLY A 205 SER A 209 0
SHEET 2 B 7 GLU A 260 VAL A 265 -1 O VAL A 262 N LEU A 207
SHEET 3 B 7 LEU A 153 ALA A 157 -1 N LEU A 153 O VAL A 265
SHEET 4 B 7 LEU A 284 VAL A 291 -1 O PHE A 285 N LEU A 156
SHEET 5 B 7 GLY A 226 VAL A 229 -1 N GLY A 226 O VAL A 291
SHEET 6 B 7 VAL A 296 LEU A 298 1 O TYR A 297 N VAL A 229
SHEET 7 B 7 ALA A 301 PRO A 302 -1 O ALA A 301 N LEU A 298
SHEET 1 C 5 GLY B 33 TRP B 36 0
SHEET 2 C 5 ALA B 41 LEU B 50 -1 O TRP B 42 N VAL B 35
SHEET 3 C 5 ALA B 131 ALA B 140 -1 O VAL B 134 N ASP B 47
SHEET 4 C 5 ARG B 82 LEU B 92 -1 N THR B 87 O SER B 135
SHEET 5 C 5 PHE B 118 ARG B 126 1 O ASN B 125 N LEU B 92
SHEET 1 D 7 GLY B 205 SER B 209 0
SHEET 2 D 7 GLU B 260 VAL B 265 -1 O VAL B 262 N LEU B 207
SHEET 3 D 7 LEU B 153 ALA B 157 -1 N LEU B 153 O VAL B 265
SHEET 4 D 7 LEU B 284 VAL B 291 -1 O GLY B 288 N LEU B 154
SHEET 5 D 7 GLY B 226 VAL B 229 -1 N GLY B 226 O VAL B 291
SHEET 6 D 7 VAL B 296 LEU B 298 1 O TYR B 297 N VAL B 229
SHEET 7 D 7 ALA B 301 PRO B 302 -1 O ALA B 301 N LEU B 298
SHEET 1 E 5 GLY C 33 ALA C 37 0
SHEET 2 E 5 ARG C 40 LEU C 50 -1 O ARG C 40 N ALA C 37
SHEET 3 E 5 ALA C 131 ALA C 140 -1 O VAL C 134 N ASP C 47
SHEET 4 E 5 ARG C 82 LEU C 92 -1 N PHE C 91 O ALA C 131
SHEET 5 E 5 PHE C 118 ARG C 126 1 O ASN C 125 N LEU C 92
SHEET 1 F 7 GLY C 205 SER C 209 0
SHEET 2 F 7 GLU C 260 VAL C 265 -1 O VAL C 262 N LEU C 207
SHEET 3 F 7 LEU C 153 ALA C 157 -1 N LEU C 153 O VAL C 265
SHEET 4 F 7 LEU C 284 VAL C 291 -1 O PHE C 285 N LEU C 156
SHEET 5 F 7 GLY C 226 VAL C 229 -1 N GLY C 226 O VAL C 291
SHEET 6 F 7 VAL C 296 LEU C 298 1 O TYR C 297 N VAL C 229
SHEET 7 F 7 ALA C 301 PRO C 302 -1 O ALA C 301 N LEU C 298
SHEET 1 G 5 GLY D 33 ALA D 37 0
SHEET 2 G 5 ARG D 40 LEU D 50 -1 O ARG D 40 N ALA D 37
SHEET 3 G 5 ALA D 131 ALA D 140 -1 O ALA D 140 N ALA D 41
SHEET 4 G 5 ARG D 82 LEU D 92 -1 N GLY D 89 O THR D 133
SHEET 5 G 5 LEU D 119 ARG D 126 1 O LEU D 120 N PHE D 86
SHEET 1 H 7 GLY D 205 SER D 209 0
SHEET 2 H 7 GLU D 260 VAL D 265 -1 O VAL D 262 N LEU D 207
SHEET 3 H 7 LEU D 153 ALA D 157 -1 N LEU D 153 O VAL D 265
SHEET 4 H 7 LEU D 284 VAL D 291 -1 O ALA D 287 N LEU D 154
SHEET 5 H 7 GLY D 226 VAL D 229 -1 N GLU D 228 O ARG D 289
SHEET 6 H 7 GLY D 295 LEU D 298 1 O TYR D 297 N VAL D 229
SHEET 7 H 7 ALA D 301 PRO D 302 -1 O ALA D 301 N LEU D 298
CRYST1 141.564 52.190 181.124 90.00 108.33 90.00 C 1 2 1 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 0.007064 0.000000 0.002340 0.00000
SCALE2 0.000000 0.019161 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005816 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
