HEADER OXIDOREDUCTASE 02-SEP-05 2D1Y
TITLE CRYSTAL STRUCTURE OF TT0321 FROM THERMUS THERMOPHILUS HB8
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HYPOTHETICAL PROTEIN TT0321;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: THERMUS THERMOPHILUS;
SOURCE 3 ORGANISM_TAXID: 274;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 6 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PET11A
KEYWDS STRUCRTURAL GENOMICS, THERMUS THERMOPHILUS HB8, STRUCTURAL GENOMICS,
KEYWDS 2 NPPSFA, NATIONAL PROJECT ON PROTEIN STRUCTURAL AND FUNCTIONAL
KEYWDS 3 ANALYSES, RIKEN STRUCTURAL GENOMICS/PROTEOMICS INITIATIVE, RSGI,
KEYWDS 4 OXIDOREDUCTASE
EXPDTA X-RAY DIFFRACTION
AUTHOR Y.ASADA,N.KUNISHIMA,RIKEN STRUCTURAL GENOMICS/PROTEOMICS INITIATIVE
AUTHOR 2 (RSGI)
REVDAT 4 25-OCT-23 2D1Y 1 REMARK
REVDAT 3 03-NOV-21 2D1Y 1 JRNL REMARK
REVDAT 2 24-FEB-09 2D1Y 1 VERSN
REVDAT 1 02-MAR-06 2D1Y 0
JRNL AUTH Y.ASADA,S.ENDO,Y.INOUE,H.MAMIYA,A.HARA,N.KUNISHIMA,
JRNL AUTH 2 T.MATSUNAGA
JRNL TITL BIOCHEMICAL AND STRUCTURAL CHARACTERIZATION OF A SHORT-CHAIN
JRNL TITL 2 DEHYDROGENASE/REDUCTASE OF THERMUS THERMOPHILUS HB8: A
JRNL TITL 3 HYPERTHERMOSTABLE ALDOSE-1-DEHYDROGENASE WITH BROAD
JRNL TITL 4 SUBSTRATE SPECIFICITY.
JRNL REF CHEM.BIOL.INTERACT. V. 178 117 2009
JRNL REFN ISSN 0009-2797
JRNL PMID 18926808
JRNL DOI 10.1016/J.CBI.2008.09.018
REMARK 2
REMARK 2 RESOLUTION. 1.65 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) : 1.65
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 28.93
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) (%) : 99.7
REMARK 3 NUMBER OF REFLECTIONS : 108767
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RAMDOM
REMARK 3 R VALUE (WORKING SET) : 0.175
REMARK 3 FREE R VALUE : 0.194
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : 5439
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) : 1.65
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.73
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 98.80
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.2210
REMARK 3 BIN FREE R VALUE : 0.2310
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 665
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 : 7183
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 176
REMARK 3 SOLVENT ATOMS : 827
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 16.76
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 21.70
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -6.37000
REMARK 3 B22 (A**2) : 6.99000
REMARK 3 B33 (A**2) : -0.62000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -0.67000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.16
REMARK 3 ESD FROM SIGMAA (A) : 0.13
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) : 0.18
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.15
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.005
REMARK 3 BOND ANGLES (DEGREES) : 1.200
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 21.10
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.830
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) : 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 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : NULL
REMARK 3 KSOL : NULL
REMARK 3 BSOL : NULL
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 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2D1Y COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 05-SEP-05.
REMARK 100 THE DEPOSITION ID IS D_1000024887.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 07-FEB-05
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SPRING-8
REMARK 200 BEAMLINE : 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 : BENDING MAGNET
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS V
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 108794
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.650
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 3.500
REMARK 200 R MERGE (I) : 0.06400
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 12.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.65
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.71
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 3.50
REMARK 200 R MERGE FOR SHELL (I) : 0.30800
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 4.290
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: 1IPE.PDB
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 38.12
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.00
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2M MAGNESIUM CHLORIDE HEXAHYDRATE,
REMARK 280 0.1M TRIS-HCL, 30% W/V PEG 4000, PH 8.5, MICROBATCH, TEMPERATURE
REMARK 280 291K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,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 47.66700
REMARK 290 SMTRY3 2 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 300 REMARK: THE BIOLOGICAL ASSEMBLY IS TETRAMER
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
REMARK 350 TOTAL BURIED SURFACE AREA: 17810 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 32620 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -132.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, 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 MET A 1
REMARK 465 LEU A 193
REMARK 465 SER A 194
REMARK 465 PRO A 195
REMARK 465 ASP A 196
REMARK 465 PRO A 197
REMARK 465 GLU A 198
REMARK 465 ARG A 199
REMARK 465 THR A 200
REMARK 465 MET A 250
REMARK 465 MET A 251
REMARK 465 ALA A 252
REMARK 465 GLY A 253
REMARK 465 ARG A 254
REMARK 465 PRO A 255
REMARK 465 VAL A 256
REMARK 465 MET B 1
REMARK 465 ALA B 192
REMARK 465 LEU B 193
REMARK 465 SER B 194
REMARK 465 PRO B 195
REMARK 465 ASP B 196
REMARK 465 PRO B 197
REMARK 465 GLU B 198
REMARK 465 MET B 251
REMARK 465 ALA B 252
REMARK 465 GLY B 253
REMARK 465 ARG B 254
REMARK 465 PRO B 255
REMARK 465 VAL B 256
REMARK 465 MET C 1
REMARK 465 MET C 250
REMARK 465 MET C 251
REMARK 465 ALA C 252
REMARK 465 GLY C 253
REMARK 465 ARG C 254
REMARK 465 PRO C 255
REMARK 465 VAL C 256
REMARK 465 MET D 1
REMARK 465 GLY D 2
REMARK 465 LEU D 193
REMARK 465 SER D 194
REMARK 465 PRO D 195
REMARK 465 ASP D 196
REMARK 465 PRO D 197
REMARK 465 GLU D 198
REMARK 465 ARG D 199
REMARK 465 MET D 250
REMARK 465 MET D 251
REMARK 465 ALA D 252
REMARK 465 GLY D 253
REMARK 465 ARG D 254
REMARK 465 PRO D 255
REMARK 465 VAL D 256
REMARK 480
REMARK 480 ZERO OCCUPANCY ATOM
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 480 M RES C SSEQI ATOMS
REMARK 480 GLU A 185 CG CD OE1 OE2
REMARK 480 ARG B 124 CD NE CZ NH1 NH2
REMARK 480 GLU B 229 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 ALA A 135 -132.41 -90.36
REMARK 500 ASN A 146 40.11 -148.69
REMARK 500 LEU B 109 -51.75 -124.24
REMARK 500 ALA B 135 -130.43 -91.80
REMARK 500 ASN B 146 39.17 -148.77
REMARK 500 ASP B 206 4.33 -69.77
REMARK 500 ALA C 135 -131.13 -93.23
REMARK 500 ASN C 146 41.38 -148.74
REMARK 500 ALA D 135 -131.95 -91.96
REMARK 500 ASN D 146 39.61 -148.89
REMARK 500 LEU D 188 36.86 -79.53
REMARK 500 GLU D 189 -47.46 -143.66
REMARK 500 ARG D 201 -73.40 -52.46
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 NAD A 1001
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAD B 1002
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAD C 1003
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAD D 1004
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: TTK003000321.1 RELATED DB: TARGETDB
DBREF 2D1Y A 1 256 UNP Q5SLC4 Q5SLC4_THET8 1 256
DBREF 2D1Y B 1 256 UNP Q5SLC4 Q5SLC4_THET8 1 256
DBREF 2D1Y C 1 256 UNP Q5SLC4 Q5SLC4_THET8 1 256
DBREF 2D1Y D 1 256 UNP Q5SLC4 Q5SLC4_THET8 1 256
SEQRES 1 A 256 MET GLY LEU PHE ALA GLY LYS GLY VAL LEU VAL THR GLY
SEQRES 2 A 256 GLY ALA ARG GLY ILE GLY ARG ALA ILE ALA GLN ALA PHE
SEQRES 3 A 256 ALA ARG GLU GLY ALA LEU VAL ALA LEU CYS ASP LEU ARG
SEQRES 4 A 256 PRO GLU GLY LYS GLU VAL ALA GLU ALA ILE GLY GLY ALA
SEQRES 5 A 256 PHE PHE GLN VAL ASP LEU GLU ASP GLU ARG GLU ARG VAL
SEQRES 6 A 256 ARG PHE VAL GLU GLU ALA ALA TYR ALA LEU GLY ARG VAL
SEQRES 7 A 256 ASP VAL LEU VAL ASN ASN ALA ALA ILE ALA ALA PRO GLY
SEQRES 8 A 256 SER ALA LEU THR VAL ARG LEU PRO GLU TRP ARG ARG VAL
SEQRES 9 A 256 LEU GLU VAL ASN LEU THR ALA PRO MET HIS LEU SER ALA
SEQRES 10 A 256 LEU ALA ALA ARG GLU MET ARG LYS VAL GLY GLY GLY ALA
SEQRES 11 A 256 ILE VAL ASN VAL ALA SER VAL GLN GLY LEU PHE ALA GLU
SEQRES 12 A 256 GLN GLU ASN ALA ALA TYR ASN ALA SER LYS GLY GLY LEU
SEQRES 13 A 256 VAL ASN LEU THR ARG SER LEU ALA LEU ASP LEU ALA PRO
SEQRES 14 A 256 LEU ARG ILE ARG VAL ASN ALA VAL ALA PRO GLY ALA ILE
SEQRES 15 A 256 ALA THR GLU ALA VAL LEU GLU ALA ILE ALA LEU SER PRO
SEQRES 16 A 256 ASP PRO GLU ARG THR ARG ARG ASP TRP GLU ASP LEU HIS
SEQRES 17 A 256 ALA LEU ARG ARG LEU GLY LYS PRO GLU GLU VAL ALA GLU
SEQRES 18 A 256 ALA VAL LEU PHE LEU ALA SER GLU LYS ALA SER PHE ILE
SEQRES 19 A 256 THR GLY ALA ILE LEU PRO VAL ASP GLY GLY MET THR ALA
SEQRES 20 A 256 SER PHE MET MET ALA GLY ARG PRO VAL
SEQRES 1 B 256 MET GLY LEU PHE ALA GLY LYS GLY VAL LEU VAL THR GLY
SEQRES 2 B 256 GLY ALA ARG GLY ILE GLY ARG ALA ILE ALA GLN ALA PHE
SEQRES 3 B 256 ALA ARG GLU GLY ALA LEU VAL ALA LEU CYS ASP LEU ARG
SEQRES 4 B 256 PRO GLU GLY LYS GLU VAL ALA GLU ALA ILE GLY GLY ALA
SEQRES 5 B 256 PHE PHE GLN VAL ASP LEU GLU ASP GLU ARG GLU ARG VAL
SEQRES 6 B 256 ARG PHE VAL GLU GLU ALA ALA TYR ALA LEU GLY ARG VAL
SEQRES 7 B 256 ASP VAL LEU VAL ASN ASN ALA ALA ILE ALA ALA PRO GLY
SEQRES 8 B 256 SER ALA LEU THR VAL ARG LEU PRO GLU TRP ARG ARG VAL
SEQRES 9 B 256 LEU GLU VAL ASN LEU THR ALA PRO MET HIS LEU SER ALA
SEQRES 10 B 256 LEU ALA ALA ARG GLU MET ARG LYS VAL GLY GLY GLY ALA
SEQRES 11 B 256 ILE VAL ASN VAL ALA SER VAL GLN GLY LEU PHE ALA GLU
SEQRES 12 B 256 GLN GLU ASN ALA ALA TYR ASN ALA SER LYS GLY GLY LEU
SEQRES 13 B 256 VAL ASN LEU THR ARG SER LEU ALA LEU ASP LEU ALA PRO
SEQRES 14 B 256 LEU ARG ILE ARG VAL ASN ALA VAL ALA PRO GLY ALA ILE
SEQRES 15 B 256 ALA THR GLU ALA VAL LEU GLU ALA ILE ALA LEU SER PRO
SEQRES 16 B 256 ASP PRO GLU ARG THR ARG ARG ASP TRP GLU ASP LEU HIS
SEQRES 17 B 256 ALA LEU ARG ARG LEU GLY LYS PRO GLU GLU VAL ALA GLU
SEQRES 18 B 256 ALA VAL LEU PHE LEU ALA SER GLU LYS ALA SER PHE ILE
SEQRES 19 B 256 THR GLY ALA ILE LEU PRO VAL ASP GLY GLY MET THR ALA
SEQRES 20 B 256 SER PHE MET MET ALA GLY ARG PRO VAL
SEQRES 1 C 256 MET GLY LEU PHE ALA GLY LYS GLY VAL LEU VAL THR GLY
SEQRES 2 C 256 GLY ALA ARG GLY ILE GLY ARG ALA ILE ALA GLN ALA PHE
SEQRES 3 C 256 ALA ARG GLU GLY ALA LEU VAL ALA LEU CYS ASP LEU ARG
SEQRES 4 C 256 PRO GLU GLY LYS GLU VAL ALA GLU ALA ILE GLY GLY ALA
SEQRES 5 C 256 PHE PHE GLN VAL ASP LEU GLU ASP GLU ARG GLU ARG VAL
SEQRES 6 C 256 ARG PHE VAL GLU GLU ALA ALA TYR ALA LEU GLY ARG VAL
SEQRES 7 C 256 ASP VAL LEU VAL ASN ASN ALA ALA ILE ALA ALA PRO GLY
SEQRES 8 C 256 SER ALA LEU THR VAL ARG LEU PRO GLU TRP ARG ARG VAL
SEQRES 9 C 256 LEU GLU VAL ASN LEU THR ALA PRO MET HIS LEU SER ALA
SEQRES 10 C 256 LEU ALA ALA ARG GLU MET ARG LYS VAL GLY GLY GLY ALA
SEQRES 11 C 256 ILE VAL ASN VAL ALA SER VAL GLN GLY LEU PHE ALA GLU
SEQRES 12 C 256 GLN GLU ASN ALA ALA TYR ASN ALA SER LYS GLY GLY LEU
SEQRES 13 C 256 VAL ASN LEU THR ARG SER LEU ALA LEU ASP LEU ALA PRO
SEQRES 14 C 256 LEU ARG ILE ARG VAL ASN ALA VAL ALA PRO GLY ALA ILE
SEQRES 15 C 256 ALA THR GLU ALA VAL LEU GLU ALA ILE ALA LEU SER PRO
SEQRES 16 C 256 ASP PRO GLU ARG THR ARG ARG ASP TRP GLU ASP LEU HIS
SEQRES 17 C 256 ALA LEU ARG ARG LEU GLY LYS PRO GLU GLU VAL ALA GLU
SEQRES 18 C 256 ALA VAL LEU PHE LEU ALA SER GLU LYS ALA SER PHE ILE
SEQRES 19 C 256 THR GLY ALA ILE LEU PRO VAL ASP GLY GLY MET THR ALA
SEQRES 20 C 256 SER PHE MET MET ALA GLY ARG PRO VAL
SEQRES 1 D 256 MET GLY LEU PHE ALA GLY LYS GLY VAL LEU VAL THR GLY
SEQRES 2 D 256 GLY ALA ARG GLY ILE GLY ARG ALA ILE ALA GLN ALA PHE
SEQRES 3 D 256 ALA ARG GLU GLY ALA LEU VAL ALA LEU CYS ASP LEU ARG
SEQRES 4 D 256 PRO GLU GLY LYS GLU VAL ALA GLU ALA ILE GLY GLY ALA
SEQRES 5 D 256 PHE PHE GLN VAL ASP LEU GLU ASP GLU ARG GLU ARG VAL
SEQRES 6 D 256 ARG PHE VAL GLU GLU ALA ALA TYR ALA LEU GLY ARG VAL
SEQRES 7 D 256 ASP VAL LEU VAL ASN ASN ALA ALA ILE ALA ALA PRO GLY
SEQRES 8 D 256 SER ALA LEU THR VAL ARG LEU PRO GLU TRP ARG ARG VAL
SEQRES 9 D 256 LEU GLU VAL ASN LEU THR ALA PRO MET HIS LEU SER ALA
SEQRES 10 D 256 LEU ALA ALA ARG GLU MET ARG LYS VAL GLY GLY GLY ALA
SEQRES 11 D 256 ILE VAL ASN VAL ALA SER VAL GLN GLY LEU PHE ALA GLU
SEQRES 12 D 256 GLN GLU ASN ALA ALA TYR ASN ALA SER LYS GLY GLY LEU
SEQRES 13 D 256 VAL ASN LEU THR ARG SER LEU ALA LEU ASP LEU ALA PRO
SEQRES 14 D 256 LEU ARG ILE ARG VAL ASN ALA VAL ALA PRO GLY ALA ILE
SEQRES 15 D 256 ALA THR GLU ALA VAL LEU GLU ALA ILE ALA LEU SER PRO
SEQRES 16 D 256 ASP PRO GLU ARG THR ARG ARG ASP TRP GLU ASP LEU HIS
SEQRES 17 D 256 ALA LEU ARG ARG LEU GLY LYS PRO GLU GLU VAL ALA GLU
SEQRES 18 D 256 ALA VAL LEU PHE LEU ALA SER GLU LYS ALA SER PHE ILE
SEQRES 19 D 256 THR GLY ALA ILE LEU PRO VAL ASP GLY GLY MET THR ALA
SEQRES 20 D 256 SER PHE MET MET ALA GLY ARG PRO VAL
HET NAD A1001 44
HET NAD B1002 44
HET NAD C1003 44
HET NAD D1004 44
HETNAM NAD NICOTINAMIDE-ADENINE-DINUCLEOTIDE
FORMUL 5 NAD 4(C21 H27 N7 O14 P2)
FORMUL 9 HOH *827(H2 O)
HELIX 1 1 ARG A 16 GLU A 29 1 14
HELIX 2 2 GLU A 41 GLY A 50 1 10
HELIX 3 3 ASP A 60 GLY A 76 1 17
HELIX 4 4 ARG A 97 LEU A 109 1 13
HELIX 5 5 LEU A 109 LYS A 125 1 17
HELIX 6 6 SER A 136 LEU A 140 5 5
HELIX 7 7 ASN A 146 ALA A 168 1 23
HELIX 8 8 THR A 184 ALA A 192 1 9
HELIX 9 9 ARG A 201 ASP A 206 1 6
HELIX 10 10 LYS A 215 SER A 228 1 14
HELIX 11 11 GLU A 229 SER A 232 5 4
HELIX 12 12 GLY A 244 SER A 248 5 5
HELIX 13 13 ARG B 16 GLU B 29 1 14
HELIX 14 14 GLU B 41 GLY B 50 1 10
HELIX 15 15 ASP B 60 GLY B 76 1 17
HELIX 16 16 ARG B 97 LEU B 109 1 13
HELIX 17 17 LEU B 109 ARG B 124 1 16
HELIX 18 18 LYS B 125 GLY B 127 5 3
HELIX 19 19 SER B 136 LEU B 140 5 5
HELIX 20 20 ASN B 146 ALA B 168 1 23
HELIX 21 21 THR B 184 ILE B 191 1 8
HELIX 22 22 ARG B 199 ASP B 206 1 8
HELIX 23 23 LYS B 215 SER B 228 1 14
HELIX 24 24 GLU B 229 SER B 232 5 4
HELIX 25 25 GLY B 244 SER B 248 5 5
HELIX 26 26 ARG C 16 GLU C 29 1 14
HELIX 27 27 GLU C 41 ILE C 49 1 9
HELIX 28 28 ASP C 60 GLY C 76 1 17
HELIX 29 29 ARG C 97 LEU C 109 1 13
HELIX 30 30 LEU C 109 ARG C 124 1 16
HELIX 31 31 LYS C 125 GLY C 127 5 3
HELIX 32 32 SER C 136 LEU C 140 5 5
HELIX 33 33 ASN C 146 ALA C 168 1 23
HELIX 34 34 THR C 184 LEU C 193 1 10
HELIX 35 35 ASP C 196 ASP C 206 1 11
HELIX 36 36 LYS C 215 SER C 228 1 14
HELIX 37 37 GLU C 229 SER C 232 5 4
HELIX 38 38 GLY C 244 SER C 248 5 5
HELIX 39 39 ARG D 16 GLU D 29 1 14
HELIX 40 40 GLU D 41 GLY D 50 1 10
HELIX 41 41 ASP D 60 GLY D 76 1 17
HELIX 42 42 ARG D 97 LEU D 109 1 13
HELIX 43 43 LEU D 109 ARG D 124 1 16
HELIX 44 44 LYS D 125 GLY D 127 5 3
HELIX 45 45 SER D 136 LEU D 140 5 5
HELIX 46 46 ASN D 146 ALA D 168 1 23
HELIX 47 47 ALA D 186 ILE D 191 1 6
HELIX 48 48 THR D 200 ASP D 206 1 7
HELIX 49 49 LYS D 215 SER D 228 1 14
HELIX 50 50 GLU D 229 SER D 232 5 4
HELIX 51 51 GLY D 244 SER D 248 5 5
SHEET 1 A 7 ALA A 52 GLN A 55 0
SHEET 2 A 7 LEU A 32 ASP A 37 1 N VAL A 33 O ALA A 52
SHEET 3 A 7 GLY A 8 THR A 12 1 N VAL A 9 O LEU A 32
SHEET 4 A 7 VAL A 80 ASN A 83 1 O VAL A 80 N LEU A 10
SHEET 5 A 7 GLY A 129 VAL A 134 1 O VAL A 134 N ASN A 83
SHEET 6 A 7 ILE A 172 PRO A 179 1 O ASN A 175 N ASN A 133
SHEET 7 A 7 ILE A 238 VAL A 241 1 O LEU A 239 N ALA A 176
SHEET 1 B 7 ALA B 52 GLN B 55 0
SHEET 2 B 7 LEU B 32 ASP B 37 1 N VAL B 33 O ALA B 52
SHEET 3 B 7 GLY B 8 THR B 12 1 N VAL B 9 O ALA B 34
SHEET 4 B 7 VAL B 80 ASN B 83 1 O VAL B 80 N LEU B 10
SHEET 5 B 7 GLY B 129 VAL B 134 1 O VAL B 134 N ASN B 83
SHEET 6 B 7 ILE B 172 PRO B 179 1 O ASN B 175 N ASN B 133
SHEET 7 B 7 ILE B 238 VAL B 241 1 O LEU B 239 N ALA B 176
SHEET 1 C 7 ALA C 52 GLN C 55 0
SHEET 2 C 7 LEU C 32 ASP C 37 1 N VAL C 33 O ALA C 52
SHEET 3 C 7 GLY C 8 THR C 12 1 N VAL C 9 O ALA C 34
SHEET 4 C 7 VAL C 80 ASN C 83 1 O VAL C 80 N LEU C 10
SHEET 5 C 7 GLY C 129 VAL C 134 1 O VAL C 134 N ASN C 83
SHEET 6 C 7 ILE C 172 PRO C 179 1 O ASN C 175 N ASN C 133
SHEET 7 C 7 ILE C 238 VAL C 241 1 O LEU C 239 N ALA C 176
SHEET 1 D 7 ALA D 52 GLN D 55 0
SHEET 2 D 7 LEU D 32 ASP D 37 1 N VAL D 33 O ALA D 52
SHEET 3 D 7 GLY D 8 THR D 12 1 N VAL D 9 O ALA D 34
SHEET 4 D 7 VAL D 80 ASN D 83 1 O VAL D 80 N LEU D 10
SHEET 5 D 7 GLY D 129 VAL D 134 1 O VAL D 134 N ASN D 83
SHEET 6 D 7 ILE D 172 PRO D 179 1 O ASN D 175 N ASN D 133
SHEET 7 D 7 ILE D 238 VAL D 241 1 O LEU D 239 N ALA D 176
SITE 1 AC1 29 GLY A 13 ARG A 16 GLY A 17 ILE A 18
SITE 2 AC1 29 ASP A 37 LEU A 38 ARG A 39 VAL A 56
SITE 3 AC1 29 ASP A 57 LEU A 58 ASN A 84 ALA A 85
SITE 4 AC1 29 ALA A 86 ILE A 87 VAL A 134 ALA A 135
SITE 5 AC1 29 SER A 136 TYR A 149 LYS A 153 PRO A 179
SITE 6 AC1 29 GLY A 180 ILE A 182 THR A 184 ALA A 186
SITE 7 AC1 29 VAL A 187 HOH A1028 HOH A1044 HOH A1096
SITE 8 AC1 29 HOH A1104
SITE 1 AC2 28 GLY B 13 ARG B 16 GLY B 17 ILE B 18
SITE 2 AC2 28 ASP B 37 LEU B 38 ARG B 39 VAL B 56
SITE 3 AC2 28 ASP B 57 LEU B 58 ASN B 84 ALA B 85
SITE 4 AC2 28 ALA B 86 ILE B 87 VAL B 134 ALA B 135
SITE 5 AC2 28 SER B 136 TYR B 149 LYS B 153 PRO B 179
SITE 6 AC2 28 GLY B 180 ILE B 182 THR B 184 VAL B 187
SITE 7 AC2 28 HOH B1043 HOH B1079 HOH B1090 HOH B1127
SITE 1 AC3 31 GLY C 13 ARG C 16 GLY C 17 ILE C 18
SITE 2 AC3 31 ASP C 37 LEU C 38 ARG C 39 VAL C 56
SITE 3 AC3 31 ASP C 57 LEU C 58 ASN C 84 ALA C 85
SITE 4 AC3 31 ALA C 86 ILE C 87 VAL C 134 ALA C 135
SITE 5 AC3 31 SER C 136 TYR C 149 LYS C 153 PRO C 179
SITE 6 AC3 31 GLY C 180 ALA C 181 ILE C 182 THR C 184
SITE 7 AC3 31 ALA C 186 VAL C 187 HOH C1006 HOH C1007
SITE 8 AC3 31 HOH C1049 HOH C1077 HOH C1150
SITE 1 AC4 31 GLY D 13 ARG D 16 GLY D 17 ILE D 18
SITE 2 AC4 31 ASP D 37 LEU D 38 ARG D 39 VAL D 56
SITE 3 AC4 31 ASP D 57 LEU D 58 ASN D 84 ALA D 85
SITE 4 AC4 31 ALA D 86 ILE D 87 VAL D 134 ALA D 135
SITE 5 AC4 31 SER D 136 TYR D 149 LYS D 153 PRO D 179
SITE 6 AC4 31 GLY D 180 ALA D 181 ILE D 182 THR D 184
SITE 7 AC4 31 ALA D 186 VAL D 187 HOH D1020 HOH D1039
SITE 8 AC4 31 HOH D1052 HOH D1109 HOH D1157
CRYST1 71.391 95.334 71.409 90.00 108.25 90.00 P 1 21 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 0.014007 0.000000 0.004620 0.00000
SCALE2 0.000000 0.010489 0.000000 0.00000
SCALE3 0.000000 0.000000 0.014746 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
