HEADER OXIDOREDUCTASE 29-MAR-07 2EP5
TITLE STRUCTURAL STUDY OF PROJECT ID ST1242 FROM SULFOLOBUS TOKODAII STRAIN7
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: 350AA LONG HYPOTHETICAL ASPARTATE-SEMIALDEHYDE
COMPND 3 DEHYDROGENASE;
COMPND 4 CHAIN: A, B, C, D;
COMPND 5 EC: 1.2.1.11;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SULFOLOBUS TOKODAII;
SOURCE 3 ORGANISM_TAXID: 111955;
SOURCE 4 STRAIN: STRAIN7;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL-21 CODONPLUS(DE3)-RIL;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET21D
KEYWDS OXIDOREDUCTASE, STRUCTURAL GENOMICS, NPPSFA, NATIONAL PROJECT ON
KEYWDS 2 PROTEIN STRUCTURAL AND FUNCTIONAL ANALYSES, RIKEN STRUCTURAL
KEYWDS 3 GENOMICS/PROTEOMICS INITIATIVE, RSGI
EXPDTA X-RAY DIFFRACTION
AUTHOR Y.ASADA,N.KUNISHIMA,RIKEN STRUCTURAL GENOMICS/PROTEOMICS INITIATIVE
AUTHOR 2 (RSGI)
REVDAT 4 13-MAR-24 2EP5 1 REMARK
REVDAT 3 13-JUL-11 2EP5 1 VERSN
REVDAT 2 24-FEB-09 2EP5 1 VERSN
REVDAT 1 02-OCT-07 2EP5 0
JRNL AUTH Y.ASADA,N.KUNISHIMA
JRNL TITL STRUCTURAL STUDY OF PROJECT ID ST1242 FROM SULFOLOBUS
JRNL TITL 2 TOKODAII STRAIN7
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.40 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) : 2.40
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 29.27
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) (%) : 94.3
REMARK 3 NUMBER OF REFLECTIONS : 58141
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) : 0.191
REMARK 3 FREE R VALUE : 0.242
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : 2901
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) : 2.40
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.51
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 88.80
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.2280
REMARK 3 BIN FREE R VALUE : 0.2880
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 348
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 : 10823
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 677
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 34.17
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 30.50
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -3.40000
REMARK 3 B22 (A**2) : 7.19000
REMARK 3 B33 (A**2) : -3.79000
REMARK 3 B12 (A**2) : 4.73000
REMARK 3 B13 (A**2) : -2.31000
REMARK 3 B23 (A**2) : -2.25000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.25
REMARK 3 ESD FROM SIGMAA (A) : 0.23
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) : 0.34
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.31
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.006
REMARK 3 BOND ANGLES (DEGREES) : 1.400
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 23.90
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.870
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 2EP5 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 07-JUN-07.
REMARK 100 THE DEPOSITION ID IS D_1000026934.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 06-OCT-06
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 4.6
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) : 1.00
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : RIGAKU JUPITER 210
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 58141
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.400
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 (%) : 94.8
REMARK 200 DATA REDUNDANCY : 2.300
REMARK 200 R MERGE (I) : 0.06300
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 11.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.40
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.49
REMARK 200 COMPLETENESS FOR SHELL (%) : 94.4
REMARK 200 DATA REDUNDANCY IN SHELL : 2.30
REMARK 200 R MERGE FOR SHELL (I) : 0.19300
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 4.180
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: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 53.33
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.64
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 8W/V(%) PEG 4K, 0.1M ACET, PH 4.6,
REMARK 280 MICROBATCH, TEMPERATURE 291K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,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
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: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA,PQS
REMARK 350 TOTAL BURIED SURFACE AREA: 9830 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 50790 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -55.0 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 MET B 1
REMARK 465 MET C 1
REMARK 465 MET D 1
REMARK 465 ALA D 2
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
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,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
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 ATM2 ATM3
REMARK 500 PRO B 122 C - N - CA ANGL. DEV. = 9.1 DEGREES
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 111 -11.16 77.75
REMARK 500 PRO A 122 -72.96 -18.82
REMARK 500 ASN A 125 50.71 -145.05
REMARK 500 LYS A 169 62.48 -104.59
REMARK 500 PRO A 199 24.53 -69.60
REMARK 500 LYS A 202 123.36 -37.28
REMARK 500 GLU A 316 -168.77 -113.48
REMARK 500 VAL A 330 -77.33 -99.29
REMARK 500 ALA A 333 -86.96 -159.52
REMARK 500 PHE B 111 -3.64 73.92
REMARK 500 PRO B 122 -74.35 -9.08
REMARK 500 ASN B 125 42.00 -147.90
REMARK 500 PRO B 162 0.67 -66.47
REMARK 500 LYS B 169 58.02 -105.06
REMARK 500 PRO B 199 36.86 -65.90
REMARK 500 LYS B 202 119.74 -34.55
REMARK 500 ALA B 302 120.03 -39.32
REMARK 500 VAL B 330 -79.97 -98.80
REMARK 500 ALA B 333 -79.21 -161.04
REMARK 500 PHE C 111 -2.35 72.38
REMARK 500 PRO C 122 -67.52 -16.78
REMARK 500 ASN C 125 41.24 -152.37
REMARK 500 LYS C 169 46.26 -105.87
REMARK 500 PRO C 199 40.37 -73.23
REMARK 500 LYS C 202 115.44 -35.11
REMARK 500 ALA C 302 120.43 -34.36
REMARK 500 ASN C 317 -69.37 -171.65
REMARK 500 VAL C 330 -69.63 -102.44
REMARK 500 ALA C 333 -79.24 -158.39
REMARK 500 PRO D 122 -76.92 -9.09
REMARK 500 ASN D 125 54.94 -157.77
REMARK 500 PRO D 199 39.55 -70.80
REMARK 500 LYS D 202 115.77 -28.79
REMARK 500 VAL D 330 -69.28 -105.50
REMARK 500 ALA D 333 -78.07 -162.10
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: STO001001242.1 RELATED DB: TARGETDB
DBREF 2EP5 A 1 350 UNP Q971Y6 Q971Y6_SULTO 1 350
DBREF 2EP5 B 1 350 UNP Q971Y6 Q971Y6_SULTO 1 350
DBREF 2EP5 C 1 350 UNP Q971Y6 Q971Y6_SULTO 1 350
DBREF 2EP5 D 1 350 UNP Q971Y6 Q971Y6_SULTO 1 350
SEQRES 1 A 350 MET ALA ASP LYS ILE LYS VAL SER LEU LEU GLY SER THR
SEQRES 2 A 350 GLY MET VAL GLY GLN LYS MET VAL LYS MET LEU ALA LYS
SEQRES 3 A 350 HIS PRO TYR LEU GLU LEU VAL LYS VAL SER ALA SER PRO
SEQRES 4 A 350 SER LYS ILE GLY LYS LYS TYR LYS ASP ALA VAL LYS TRP
SEQRES 5 A 350 ILE GLU GLN GLY ASP ILE PRO GLU GLU VAL GLN ASP LEU
SEQRES 6 A 350 PRO ILE VAL SER THR ASN TYR GLU ASP HIS LYS ASP VAL
SEQRES 7 A 350 ASP VAL VAL LEU SER ALA LEU PRO ASN GLU LEU ALA GLU
SEQRES 8 A 350 SER ILE GLU LEU GLU LEU VAL LYS ASN GLY LYS ILE VAL
SEQRES 9 A 350 VAL SER ASN ALA SER PRO PHE ARG MET ASP PRO ASP VAL
SEQRES 10 A 350 PRO LEU ILE ASN PRO GLU ILE ASN TRP GLU HIS LEU GLU
SEQRES 11 A 350 LEU LEU LYS PHE GLN LYS GLU ARG LYS GLY TRP LYS GLY
SEQRES 12 A 350 ILE LEU VAL LYS ASN PRO ASN CYS THR ALA ALA ILE MET
SEQRES 13 A 350 SER MET PRO ILE LYS PRO LEU ILE GLU ILE ALA THR LYS
SEQRES 14 A 350 SER LYS ILE ILE ILE THR THR LEU GLN ALA VAL SER GLY
SEQRES 15 A 350 ALA GLY TYR ASN GLY ILE SER PHE MET ALA ILE GLU GLY
SEQRES 16 A 350 ASN ILE ILE PRO TYR ILE LYS GLY GLU GLU ASP LYS ILE
SEQRES 17 A 350 ALA LYS GLU LEU THR LYS LEU ASN GLY LYS LEU GLU ASN
SEQRES 18 A 350 ASN GLN ILE ILE PRO ALA ASN LEU ASP SER THR VAL THR
SEQRES 19 A 350 SER ILE ARG VAL PRO THR ARG VAL GLY HIS MET GLY VAL
SEQRES 20 A 350 ILE ASN ILE VAL THR ASN GLU ARG ILE ASN ILE GLU GLU
SEQRES 21 A 350 ILE LYS LYS THR LEU LYS ASN PHE LYS SER LEU PRO GLN
SEQRES 22 A 350 GLN LYS ASN LEU PRO THR ALA PRO LYS GLN PRO ILE ILE
SEQRES 23 A 350 VAL ARG ASP GLU GLU ASP ARG PRO GLN PRO ILE ILE ASP
SEQRES 24 A 350 VAL ASN ALA GLU SER GLY MET ALA VAL THR VAL GLY ARG
SEQRES 25 A 350 ILE ARG HIS GLU ASN ASN VAL LEU ARG LEU VAL VAL LEU
SEQRES 26 A 350 GLY ASP ASN LEU VAL ARG GLY ALA ALA GLY ILE THR ILE
SEQRES 27 A 350 LEU THR VAL GLU VAL MET LYS GLU LEU GLY TYR ILE
SEQRES 1 B 350 MET ALA ASP LYS ILE LYS VAL SER LEU LEU GLY SER THR
SEQRES 2 B 350 GLY MET VAL GLY GLN LYS MET VAL LYS MET LEU ALA LYS
SEQRES 3 B 350 HIS PRO TYR LEU GLU LEU VAL LYS VAL SER ALA SER PRO
SEQRES 4 B 350 SER LYS ILE GLY LYS LYS TYR LYS ASP ALA VAL LYS TRP
SEQRES 5 B 350 ILE GLU GLN GLY ASP ILE PRO GLU GLU VAL GLN ASP LEU
SEQRES 6 B 350 PRO ILE VAL SER THR ASN TYR GLU ASP HIS LYS ASP VAL
SEQRES 7 B 350 ASP VAL VAL LEU SER ALA LEU PRO ASN GLU LEU ALA GLU
SEQRES 8 B 350 SER ILE GLU LEU GLU LEU VAL LYS ASN GLY LYS ILE VAL
SEQRES 9 B 350 VAL SER ASN ALA SER PRO PHE ARG MET ASP PRO ASP VAL
SEQRES 10 B 350 PRO LEU ILE ASN PRO GLU ILE ASN TRP GLU HIS LEU GLU
SEQRES 11 B 350 LEU LEU LYS PHE GLN LYS GLU ARG LYS GLY TRP LYS GLY
SEQRES 12 B 350 ILE LEU VAL LYS ASN PRO ASN CYS THR ALA ALA ILE MET
SEQRES 13 B 350 SER MET PRO ILE LYS PRO LEU ILE GLU ILE ALA THR LYS
SEQRES 14 B 350 SER LYS ILE ILE ILE THR THR LEU GLN ALA VAL SER GLY
SEQRES 15 B 350 ALA GLY TYR ASN GLY ILE SER PHE MET ALA ILE GLU GLY
SEQRES 16 B 350 ASN ILE ILE PRO TYR ILE LYS GLY GLU GLU ASP LYS ILE
SEQRES 17 B 350 ALA LYS GLU LEU THR LYS LEU ASN GLY LYS LEU GLU ASN
SEQRES 18 B 350 ASN GLN ILE ILE PRO ALA ASN LEU ASP SER THR VAL THR
SEQRES 19 B 350 SER ILE ARG VAL PRO THR ARG VAL GLY HIS MET GLY VAL
SEQRES 20 B 350 ILE ASN ILE VAL THR ASN GLU ARG ILE ASN ILE GLU GLU
SEQRES 21 B 350 ILE LYS LYS THR LEU LYS ASN PHE LYS SER LEU PRO GLN
SEQRES 22 B 350 GLN LYS ASN LEU PRO THR ALA PRO LYS GLN PRO ILE ILE
SEQRES 23 B 350 VAL ARG ASP GLU GLU ASP ARG PRO GLN PRO ILE ILE ASP
SEQRES 24 B 350 VAL ASN ALA GLU SER GLY MET ALA VAL THR VAL GLY ARG
SEQRES 25 B 350 ILE ARG HIS GLU ASN ASN VAL LEU ARG LEU VAL VAL LEU
SEQRES 26 B 350 GLY ASP ASN LEU VAL ARG GLY ALA ALA GLY ILE THR ILE
SEQRES 27 B 350 LEU THR VAL GLU VAL MET LYS GLU LEU GLY TYR ILE
SEQRES 1 C 350 MET ALA ASP LYS ILE LYS VAL SER LEU LEU GLY SER THR
SEQRES 2 C 350 GLY MET VAL GLY GLN LYS MET VAL LYS MET LEU ALA LYS
SEQRES 3 C 350 HIS PRO TYR LEU GLU LEU VAL LYS VAL SER ALA SER PRO
SEQRES 4 C 350 SER LYS ILE GLY LYS LYS TYR LYS ASP ALA VAL LYS TRP
SEQRES 5 C 350 ILE GLU GLN GLY ASP ILE PRO GLU GLU VAL GLN ASP LEU
SEQRES 6 C 350 PRO ILE VAL SER THR ASN TYR GLU ASP HIS LYS ASP VAL
SEQRES 7 C 350 ASP VAL VAL LEU SER ALA LEU PRO ASN GLU LEU ALA GLU
SEQRES 8 C 350 SER ILE GLU LEU GLU LEU VAL LYS ASN GLY LYS ILE VAL
SEQRES 9 C 350 VAL SER ASN ALA SER PRO PHE ARG MET ASP PRO ASP VAL
SEQRES 10 C 350 PRO LEU ILE ASN PRO GLU ILE ASN TRP GLU HIS LEU GLU
SEQRES 11 C 350 LEU LEU LYS PHE GLN LYS GLU ARG LYS GLY TRP LYS GLY
SEQRES 12 C 350 ILE LEU VAL LYS ASN PRO ASN CYS THR ALA ALA ILE MET
SEQRES 13 C 350 SER MET PRO ILE LYS PRO LEU ILE GLU ILE ALA THR LYS
SEQRES 14 C 350 SER LYS ILE ILE ILE THR THR LEU GLN ALA VAL SER GLY
SEQRES 15 C 350 ALA GLY TYR ASN GLY ILE SER PHE MET ALA ILE GLU GLY
SEQRES 16 C 350 ASN ILE ILE PRO TYR ILE LYS GLY GLU GLU ASP LYS ILE
SEQRES 17 C 350 ALA LYS GLU LEU THR LYS LEU ASN GLY LYS LEU GLU ASN
SEQRES 18 C 350 ASN GLN ILE ILE PRO ALA ASN LEU ASP SER THR VAL THR
SEQRES 19 C 350 SER ILE ARG VAL PRO THR ARG VAL GLY HIS MET GLY VAL
SEQRES 20 C 350 ILE ASN ILE VAL THR ASN GLU ARG ILE ASN ILE GLU GLU
SEQRES 21 C 350 ILE LYS LYS THR LEU LYS ASN PHE LYS SER LEU PRO GLN
SEQRES 22 C 350 GLN LYS ASN LEU PRO THR ALA PRO LYS GLN PRO ILE ILE
SEQRES 23 C 350 VAL ARG ASP GLU GLU ASP ARG PRO GLN PRO ILE ILE ASP
SEQRES 24 C 350 VAL ASN ALA GLU SER GLY MET ALA VAL THR VAL GLY ARG
SEQRES 25 C 350 ILE ARG HIS GLU ASN ASN VAL LEU ARG LEU VAL VAL LEU
SEQRES 26 C 350 GLY ASP ASN LEU VAL ARG GLY ALA ALA GLY ILE THR ILE
SEQRES 27 C 350 LEU THR VAL GLU VAL MET LYS GLU LEU GLY TYR ILE
SEQRES 1 D 350 MET ALA ASP LYS ILE LYS VAL SER LEU LEU GLY SER THR
SEQRES 2 D 350 GLY MET VAL GLY GLN LYS MET VAL LYS MET LEU ALA LYS
SEQRES 3 D 350 HIS PRO TYR LEU GLU LEU VAL LYS VAL SER ALA SER PRO
SEQRES 4 D 350 SER LYS ILE GLY LYS LYS TYR LYS ASP ALA VAL LYS TRP
SEQRES 5 D 350 ILE GLU GLN GLY ASP ILE PRO GLU GLU VAL GLN ASP LEU
SEQRES 6 D 350 PRO ILE VAL SER THR ASN TYR GLU ASP HIS LYS ASP VAL
SEQRES 7 D 350 ASP VAL VAL LEU SER ALA LEU PRO ASN GLU LEU ALA GLU
SEQRES 8 D 350 SER ILE GLU LEU GLU LEU VAL LYS ASN GLY LYS ILE VAL
SEQRES 9 D 350 VAL SER ASN ALA SER PRO PHE ARG MET ASP PRO ASP VAL
SEQRES 10 D 350 PRO LEU ILE ASN PRO GLU ILE ASN TRP GLU HIS LEU GLU
SEQRES 11 D 350 LEU LEU LYS PHE GLN LYS GLU ARG LYS GLY TRP LYS GLY
SEQRES 12 D 350 ILE LEU VAL LYS ASN PRO ASN CYS THR ALA ALA ILE MET
SEQRES 13 D 350 SER MET PRO ILE LYS PRO LEU ILE GLU ILE ALA THR LYS
SEQRES 14 D 350 SER LYS ILE ILE ILE THR THR LEU GLN ALA VAL SER GLY
SEQRES 15 D 350 ALA GLY TYR ASN GLY ILE SER PHE MET ALA ILE GLU GLY
SEQRES 16 D 350 ASN ILE ILE PRO TYR ILE LYS GLY GLU GLU ASP LYS ILE
SEQRES 17 D 350 ALA LYS GLU LEU THR LYS LEU ASN GLY LYS LEU GLU ASN
SEQRES 18 D 350 ASN GLN ILE ILE PRO ALA ASN LEU ASP SER THR VAL THR
SEQRES 19 D 350 SER ILE ARG VAL PRO THR ARG VAL GLY HIS MET GLY VAL
SEQRES 20 D 350 ILE ASN ILE VAL THR ASN GLU ARG ILE ASN ILE GLU GLU
SEQRES 21 D 350 ILE LYS LYS THR LEU LYS ASN PHE LYS SER LEU PRO GLN
SEQRES 22 D 350 GLN LYS ASN LEU PRO THR ALA PRO LYS GLN PRO ILE ILE
SEQRES 23 D 350 VAL ARG ASP GLU GLU ASP ARG PRO GLN PRO ILE ILE ASP
SEQRES 24 D 350 VAL ASN ALA GLU SER GLY MET ALA VAL THR VAL GLY ARG
SEQRES 25 D 350 ILE ARG HIS GLU ASN ASN VAL LEU ARG LEU VAL VAL LEU
SEQRES 26 D 350 GLY ASP ASN LEU VAL ARG GLY ALA ALA GLY ILE THR ILE
SEQRES 27 D 350 LEU THR VAL GLU VAL MET LYS GLU LEU GLY TYR ILE
FORMUL 5 HOH *677(H2 O)
HELIX 1 1 GLY A 14 ALA A 25 1 12
HELIX 2 2 SER A 38 ILE A 42 5 5
HELIX 3 3 LYS A 45 VAL A 50 1 6
HELIX 4 4 PRO A 59 ASP A 64 1 6
HELIX 5 5 ASN A 71 LYS A 76 5 6
HELIX 6 6 PRO A 86 ASN A 100 1 15
HELIX 7 7 ASN A 121 TRP A 126 1 6
HELIX 8 8 GLU A 127 GLU A 130 5 4
HELIX 9 9 LEU A 131 GLY A 140 1 10
HELIX 10 10 ASN A 150 LYS A 161 1 12
HELIX 11 11 LEU A 163 LYS A 169 1 7
HELIX 12 12 VAL A 180 GLY A 184 5 5
HELIX 13 13 SER A 189 GLU A 194 1 6
HELIX 14 14 GLY A 203 ASN A 216 1 14
HELIX 15 15 ASN A 257 ASN A 267 1 11
HELIX 16 16 SER A 270 LYS A 275 1 6
HELIX 17 17 GLN A 295 VAL A 300 1 6
HELIX 18 18 ASN A 301 MET A 306 5 6
HELIX 19 19 ALA A 333 LEU A 347 1 15
HELIX 20 20 GLY B 14 ALA B 25 1 12
HELIX 21 21 SER B 38 ILE B 42 5 5
HELIX 22 22 LYS B 45 ALA B 49 5 5
HELIX 23 23 ASN B 71 HIS B 75 5 5
HELIX 24 24 PRO B 86 ASN B 100 1 15
HELIX 25 25 ASN B 121 TRP B 126 1 6
HELIX 26 26 GLU B 127 LYS B 133 5 7
HELIX 27 27 PHE B 134 GLY B 140 1 7
HELIX 28 28 ASN B 150 LYS B 161 1 12
HELIX 29 29 LEU B 163 LYS B 169 1 7
HELIX 30 30 ALA B 179 GLY B 184 5 6
HELIX 31 31 SER B 189 GLU B 194 1 6
HELIX 32 32 GLY B 203 ASN B 216 1 14
HELIX 33 33 ASN B 257 ASN B 267 1 11
HELIX 34 34 SER B 270 LYS B 275 1 6
HELIX 35 35 GLN B 295 VAL B 300 1 6
HELIX 36 36 ASN B 301 MET B 306 5 6
HELIX 37 37 ALA B 333 LEU B 347 1 15
HELIX 38 38 GLY C 14 LYS C 26 1 13
HELIX 39 39 SER C 38 ILE C 42 5 5
HELIX 40 40 LYS C 45 VAL C 50 1 6
HELIX 41 41 ASN C 71 HIS C 75 5 5
HELIX 42 42 PRO C 86 ASN C 100 1 15
HELIX 43 43 ASN C 121 TRP C 126 1 6
HELIX 44 44 GLU C 127 GLU C 130 5 4
HELIX 45 45 LEU C 131 GLY C 140 1 10
HELIX 46 46 ASN C 150 LYS C 161 1 12
HELIX 47 47 LEU C 163 THR C 168 1 6
HELIX 48 48 ALA C 179 GLY C 184 5 6
HELIX 49 49 SER C 189 GLU C 194 1 6
HELIX 50 50 GLY C 203 ASN C 216 1 14
HELIX 51 51 ASN C 257 ASN C 267 1 11
HELIX 52 52 SER C 270 LYS C 275 1 6
HELIX 53 53 GLN C 295 VAL C 300 1 6
HELIX 54 54 ALA C 333 LEU C 347 1 15
HELIX 55 55 GLY D 14 ALA D 25 1 12
HELIX 56 56 SER D 38 ILE D 42 5 5
HELIX 57 57 LYS D 45 VAL D 50 1 6
HELIX 58 58 ASN D 71 HIS D 75 5 5
HELIX 59 59 PRO D 86 LYS D 99 1 14
HELIX 60 60 ASN D 121 TRP D 126 1 6
HELIX 61 61 GLU D 127 GLU D 130 5 4
HELIX 62 62 LEU D 131 GLY D 140 1 10
HELIX 63 63 ASN D 150 LYS D 161 1 12
HELIX 64 64 LEU D 163 LYS D 169 1 7
HELIX 65 65 ALA D 179 GLY D 184 5 6
HELIX 66 66 SER D 189 GLU D 194 1 6
HELIX 67 67 GLY D 203 ASN D 216 1 14
HELIX 68 68 ASN D 257 ASN D 267 1 11
HELIX 69 69 SER D 270 LYS D 275 1 6
HELIX 70 70 GLN D 295 VAL D 300 1 6
HELIX 71 71 ASN D 301 MET D 306 5 6
HELIX 72 72 ALA D 333 LEU D 347 1 15
SHEET 1 A 6 ILE A 67 VAL A 68 0
SHEET 2 A 6 LEU A 30 SER A 36 1 N VAL A 35 O VAL A 68
SHEET 3 A 6 ILE A 5 LEU A 10 1 N LEU A 9 O SER A 36
SHEET 4 A 6 VAL A 80 SER A 83 1 O LEU A 82 N LEU A 10
SHEET 5 A 6 ILE A 103 SER A 106 1 O ILE A 103 N VAL A 81
SHEET 6 A 6 ILE A 144 LYS A 147 1 O ILE A 144 N VAL A 104
SHEET 1 B 6 ASP A 230 ARG A 237 0
SHEET 2 B 6 LYS A 171 GLN A 178 1 N THR A 176 O ILE A 236
SHEET 3 B 6 HIS A 244 VAL A 251 -1 O VAL A 247 N THR A 175
SHEET 4 B 6 VAL A 319 GLY A 326 -1 O LEU A 320 N ILE A 250
SHEET 5 B 6 VAL A 308 GLU A 316 -1 N ARG A 314 O ARG A 321
SHEET 6 B 6 ILE A 285 VAL A 287 1 N ILE A 286 O VAL A 310
SHEET 1 C 2 LYS A 218 LEU A 219 0
SHEET 2 C 2 ILE A 224 ILE A 225 -1 O ILE A 225 N LYS A 218
SHEET 1 D 6 ILE B 67 VAL B 68 0
SHEET 2 D 6 LEU B 30 SER B 36 1 N VAL B 35 O VAL B 68
SHEET 3 D 6 ILE B 5 LEU B 10 1 N ILE B 5 O GLU B 31
SHEET 4 D 6 VAL B 80 SER B 83 1 O LEU B 82 N SER B 8
SHEET 5 D 6 ILE B 103 SER B 106 1 O ILE B 103 N VAL B 81
SHEET 6 D 6 ILE B 144 LYS B 147 1 O ILE B 144 N VAL B 104
SHEET 1 E 6 ASP B 230 ARG B 237 0
SHEET 2 E 6 LYS B 171 GLN B 178 1 N THR B 176 O THR B 234
SHEET 3 E 6 HIS B 244 VAL B 251 -1 O MET B 245 N LEU B 177
SHEET 4 E 6 VAL B 319 GLY B 326 -1 O VAL B 324 N GLY B 246
SHEET 5 E 6 VAL B 308 GLU B 316 -1 N THR B 309 O LEU B 325
SHEET 6 E 6 ILE B 285 ARG B 288 1 N ILE B 286 O VAL B 310
SHEET 1 F 2 LYS B 218 LEU B 219 0
SHEET 2 F 2 ILE B 224 ILE B 225 -1 O ILE B 225 N LYS B 218
SHEET 1 G 6 ILE C 67 VAL C 68 0
SHEET 2 G 6 LEU C 30 SER C 36 1 N VAL C 35 O VAL C 68
SHEET 3 G 6 ILE C 5 LEU C 10 1 N ILE C 5 O GLU C 31
SHEET 4 G 6 VAL C 80 SER C 83 1 O LEU C 82 N SER C 8
SHEET 5 G 6 ILE C 103 SER C 106 1 O ILE C 103 N VAL C 81
SHEET 6 G 6 ILE C 144 LYS C 147 1 O ILE C 144 N VAL C 104
SHEET 1 H 6 ASP C 230 ARG C 237 0
SHEET 2 H 6 LYS C 171 GLN C 178 1 N THR C 176 O ILE C 236
SHEET 3 H 6 HIS C 244 VAL C 251 -1 O VAL C 247 N THR C 175
SHEET 4 H 6 VAL C 319 GLY C 326 -1 O LEU C 320 N ILE C 250
SHEET 5 H 6 VAL C 308 HIS C 315 -1 N ARG C 314 O ARG C 321
SHEET 6 H 6 ILE C 285 VAL C 287 1 N ILE C 286 O VAL C 310
SHEET 1 I 2 LYS C 218 LEU C 219 0
SHEET 2 I 2 ILE C 224 ILE C 225 -1 O ILE C 225 N LYS C 218
SHEET 1 J 6 ILE D 67 VAL D 68 0
SHEET 2 J 6 LEU D 30 SER D 36 1 N VAL D 35 O VAL D 68
SHEET 3 J 6 ILE D 5 LEU D 10 1 N ILE D 5 O GLU D 31
SHEET 4 J 6 VAL D 80 SER D 83 1 O LEU D 82 N LEU D 10
SHEET 5 J 6 ILE D 103 SER D 106 1 O ILE D 103 N VAL D 81
SHEET 6 J 6 ILE D 144 LYS D 147 1 O VAL D 146 N VAL D 104
SHEET 1 K 6 ASP D 230 ARG D 237 0
SHEET 2 K 6 LYS D 171 GLN D 178 1 N GLN D 178 O ILE D 236
SHEET 3 K 6 HIS D 244 VAL D 251 -1 O MET D 245 N LEU D 177
SHEET 4 K 6 VAL D 319 GLY D 326 -1 O LEU D 320 N ILE D 250
SHEET 5 K 6 VAL D 308 HIS D 315 -1 N ARG D 314 O ARG D 321
SHEET 6 K 6 ILE D 285 ARG D 288 1 N ILE D 286 O VAL D 310
SHEET 1 L 2 LYS D 218 LEU D 219 0
SHEET 2 L 2 ILE D 224 ILE D 225 -1 O ILE D 225 N LYS D 218
CISPEP 1 ARG A 293 PRO A 294 0 0.24
CISPEP 2 ARG B 293 PRO B 294 0 0.40
CISPEP 3 ARG C 293 PRO C 294 0 0.12
CISPEP 4 ARG D 293 PRO D 294 0 0.06
CRYST1 70.157 73.986 91.552 68.10 68.39 86.04 P 1 4
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 0.014254 -0.000988 -0.005690 0.00000
SCALE2 0.000000 0.013548 -0.005475 0.00000
SCALE3 0.000000 0.000000 0.012671 0.00000
(ATOM LINES ARE NOT SHOWN.)
END