HEADER OXIDOREDUCTASE 28-FEB-03 1ONN
TITLE ISPC APO STRUCTURE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: 1-DEOXY-D-XYLULOSE 5-PHOSPHATE REDUCTOISOMERASE;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: 2-C-METHYL-D-ERYTHRITOL 4-PHOSPHATE SYNTHASE, ISPC;
COMPND 5 EC: 1.1.1.267;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 562;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: PQE30
KEYWDS ISOPRENOID BIOSYNTHESIS, MEVALONATE-INDEPENDENT PATHWAY, ISPC,
KEYWDS 2 OXIDOREDUCTASE
EXPDTA X-RAY DIFFRACTION
AUTHOR S.STEINBACHER,J.KAISER,W.EISENREICH,R.HUBER,A.BACHER,F.ROHDICH
REVDAT 5 25-OCT-23 1ONN 1 REMARK
REVDAT 4 24-FEB-09 1ONN 1 VERSN
REVDAT 3 13-JAN-04 1ONN 1 JRNL
REVDAT 2 20-MAY-03 1ONN 1 JRNL
REVDAT 1 18-MAR-03 1ONN 0
JRNL AUTH S.STEINBACHER,J.KAISER,W.EISENREICH,R.HUBER,A.BACHER,
JRNL AUTH 2 F.ROHDICH
JRNL TITL STRUCTURAL BASIS OF FOSMIDOMYCIN ACTION REVEALED BY THE
JRNL TITL 2 COMPLEX WITH 2-C-METHYL-D-ERYTHRITOL 4-PHOSPHATE SYNTHASE
JRNL TITL 3 (ISPC). IMPLICATIONS FOR THE CATALYTIC MECHANISM AND
JRNL TITL 4 ANTI-MALARIA DRUG DEVELOPMENT.
JRNL REF J.BIOL.CHEM. V. 278 18401 2003
JRNL REFN ISSN 0021-9258
JRNL PMID 12621040
JRNL DOI 10.1074/JBC.M300993200
REMARK 2
REMARK 2 RESOLUTION. 2.60 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS
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) : 2.60
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.00
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) (%) : 98.4
REMARK 3 NUMBER OF REFLECTIONS : 29882
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING SET) : 0.244
REMARK 3 FREE R VALUE : 0.298
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : 1557
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) : NULL
REMARK 3 BIN RESOLUTION RANGE LOW (A) : NULL
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : NULL
REMARK 3 BIN FREE R VALUE : NULL
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : NULL
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 5910
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 316
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM SIGMAA (A) : NULL
REMARK 3 LOW RESOLUTION CUTOFF (A) : NULL
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM C-V SIGMAA (A) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.011
REMARK 3 BOND ANGLES (DEGREES) : 1.410
REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL
REMARK 3 IMPROPER ANGLES (DEGREES) : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3
REMARK 3 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 1ONN COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 06-MAR-03.
REMARK 100 THE DEPOSITION ID IS D_1000018477.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 10-MAY-02
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.8
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU RU300
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.548
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : OSMIC
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 31997
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.600
REMARK 200 RESOLUTION RANGE LOW (A) : 20.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.2
REMARK 200 DATA REDUNDANCY : 3.500
REMARK 200 R MERGE (I) : 0.06200
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) : 2.60
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.70
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.4
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.40500
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: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: 1K5H
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 58.76
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.98
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 4000, PH 5.8, VAPOR DIFFUSION,
REMARK 280 SITTING DROP, TEMPERATURE 293K
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 26.70950
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 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: 3160 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 30540 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -18.0 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 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 ARG A 208
REMARK 465 HIS A 209
REMARK 465 PRO A 210
REMARK 465 ASN A 211
REMARK 465 TRP A 212
REMARK 465 SER A 213
REMARK 465 MET A 214
REMARK 465 GLY A 215
REMARK 465 SER A 398
REMARK 465 ARG B 208
REMARK 465 HIS B 209
REMARK 465 PRO B 210
REMARK 465 ASN B 211
REMARK 465 TRP B 212
REMARK 465 SER B 213
REMARK 465 MET B 214
REMARK 465 GLY B 215
REMARK 465 SER B 398
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 SER A 50 71.91 42.08
REMARK 500 ASN A 167 43.09 -146.95
REMARK 500 ASP A 197 -8.75 -161.70
REMARK 500 SER A 258 155.53 165.21
REMARK 500 TRP A 286 140.58 -37.00
REMARK 500 LYS A 366 48.38 -100.27
REMARK 500 MET A 369 -147.11 171.17
REMARK 500 PRO A 372 -173.19 -66.88
REMARK 500 GLN A 373 5.15 -159.41
REMARK 500 SER B 50 72.90 35.34
REMARK 500 LEU B 122 92.74 -68.82
REMARK 500 ASN B 167 50.05 -146.88
REMARK 500 ASP B 197 -5.46 -165.82
REMARK 500 SER B 258 157.61 163.65
REMARK 500 ASN B 288 -169.26 -103.80
REMARK 500 LYS B 301 60.45 -114.86
REMARK 500 LYS B 366 55.62 -91.70
REMARK 500 MET B 367 99.70 -160.17
REMARK 500 MET B 369 -134.29 178.62
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 TYR A 315 0.06 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1ONO RELATED DB: PDB
REMARK 900 THE SAME PROTEIN COMPLEX WITH MN2+
REMARK 900 RELATED ID: 1ONP RELATED DB: PDB
REMARK 900 THE SAME PROTEIN COMPLEX WITH MN2+ AND FOSMIDOMYCIN
DBREF 1ONN A 1 398 UNP P45568 DXR_ECOLI 1 398
DBREF 1ONN B 1 398 UNP P45568 DXR_ECOLI 1 398
SEQRES 1 A 398 MET LYS GLN LEU THR ILE LEU GLY SER THR GLY SER ILE
SEQRES 2 A 398 GLY CYS SER THR LEU ASP VAL VAL ARG HIS ASN PRO GLU
SEQRES 3 A 398 HIS PHE ARG VAL VAL ALA LEU VAL ALA GLY LYS ASN VAL
SEQRES 4 A 398 THR ARG MET VAL GLU GLN CYS LEU GLU PHE SER PRO ARG
SEQRES 5 A 398 TYR ALA VAL MET ASP ASP GLU ALA SER ALA LYS LEU LEU
SEQRES 6 A 398 LYS THR MET LEU GLN GLN GLN GLY SER ARG THR GLU VAL
SEQRES 7 A 398 LEU SER GLY GLN GLN ALA ALA CYS ASP MET ALA ALA LEU
SEQRES 8 A 398 GLU ASP VAL ASP GLN VAL MET ALA ALA ILE VAL GLY ALA
SEQRES 9 A 398 ALA GLY LEU LEU PRO THR LEU ALA ALA ILE ARG ALA GLY
SEQRES 10 A 398 LYS THR ILE LEU LEU ALA ASN LYS GLU SER LEU VAL THR
SEQRES 11 A 398 CYS GLY ARG LEU PHE MET ASP ALA VAL LYS GLN SER LYS
SEQRES 12 A 398 ALA GLN LEU LEU PRO VAL ASP SER GLU HIS ASN ALA ILE
SEQRES 13 A 398 PHE GLN SER LEU PRO GLN PRO ILE GLN HIS ASN LEU GLY
SEQRES 14 A 398 TYR ALA ASP LEU GLU GLN ASN GLY VAL VAL SER ILE LEU
SEQRES 15 A 398 LEU THR GLY SER GLY GLY PRO PHE ARG GLU THR PRO LEU
SEQRES 16 A 398 ARG ASP LEU ALA THR MET THR PRO ASP GLN ALA CYS ARG
SEQRES 17 A 398 HIS PRO ASN TRP SER MET GLY ARG LYS ILE SER VAL ASP
SEQRES 18 A 398 SER ALA THR MET MET ASN LYS GLY LEU GLU TYR ILE GLU
SEQRES 19 A 398 ALA ARG TRP LEU PHE ASN ALA SER ALA SER GLN MET GLU
SEQRES 20 A 398 VAL LEU ILE HIS PRO GLN SER VAL ILE HIS SER MET VAL
SEQRES 21 A 398 ARG TYR GLN ASP GLY SER VAL LEU ALA GLN LEU GLY GLU
SEQRES 22 A 398 PRO ASP MET ARG THR PRO ILE ALA HIS THR MET ALA TRP
SEQRES 23 A 398 PRO ASN ARG VAL ASN SER GLY VAL LYS PRO LEU ASP PHE
SEQRES 24 A 398 CYS LYS LEU SER ALA LEU THR PHE ALA ALA PRO ASP TYR
SEQRES 25 A 398 ASP ARG TYR PRO CYS LEU LYS LEU ALA MET GLU ALA PHE
SEQRES 26 A 398 GLU GLN GLY GLN ALA ALA THR THR ALA LEU ASN ALA ALA
SEQRES 27 A 398 ASN GLU ILE THR VAL ALA ALA PHE LEU ALA GLN GLN ILE
SEQRES 28 A 398 ARG PHE THR ASP ILE ALA ALA LEU ASN LEU SER VAL LEU
SEQRES 29 A 398 GLU LYS MET ASP MET ARG GLU PRO GLN CYS VAL ASP ASP
SEQRES 30 A 398 VAL LEU SER VAL ASP ALA ASN ALA ARG GLU VAL ALA ARG
SEQRES 31 A 398 LYS GLU VAL MET ARG LEU ALA SER
SEQRES 1 B 398 MET LYS GLN LEU THR ILE LEU GLY SER THR GLY SER ILE
SEQRES 2 B 398 GLY CYS SER THR LEU ASP VAL VAL ARG HIS ASN PRO GLU
SEQRES 3 B 398 HIS PHE ARG VAL VAL ALA LEU VAL ALA GLY LYS ASN VAL
SEQRES 4 B 398 THR ARG MET VAL GLU GLN CYS LEU GLU PHE SER PRO ARG
SEQRES 5 B 398 TYR ALA VAL MET ASP ASP GLU ALA SER ALA LYS LEU LEU
SEQRES 6 B 398 LYS THR MET LEU GLN GLN GLN GLY SER ARG THR GLU VAL
SEQRES 7 B 398 LEU SER GLY GLN GLN ALA ALA CYS ASP MET ALA ALA LEU
SEQRES 8 B 398 GLU ASP VAL ASP GLN VAL MET ALA ALA ILE VAL GLY ALA
SEQRES 9 B 398 ALA GLY LEU LEU PRO THR LEU ALA ALA ILE ARG ALA GLY
SEQRES 10 B 398 LYS THR ILE LEU LEU ALA ASN LYS GLU SER LEU VAL THR
SEQRES 11 B 398 CYS GLY ARG LEU PHE MET ASP ALA VAL LYS GLN SER LYS
SEQRES 12 B 398 ALA GLN LEU LEU PRO VAL ASP SER GLU HIS ASN ALA ILE
SEQRES 13 B 398 PHE GLN SER LEU PRO GLN PRO ILE GLN HIS ASN LEU GLY
SEQRES 14 B 398 TYR ALA ASP LEU GLU GLN ASN GLY VAL VAL SER ILE LEU
SEQRES 15 B 398 LEU THR GLY SER GLY GLY PRO PHE ARG GLU THR PRO LEU
SEQRES 16 B 398 ARG ASP LEU ALA THR MET THR PRO ASP GLN ALA CYS ARG
SEQRES 17 B 398 HIS PRO ASN TRP SER MET GLY ARG LYS ILE SER VAL ASP
SEQRES 18 B 398 SER ALA THR MET MET ASN LYS GLY LEU GLU TYR ILE GLU
SEQRES 19 B 398 ALA ARG TRP LEU PHE ASN ALA SER ALA SER GLN MET GLU
SEQRES 20 B 398 VAL LEU ILE HIS PRO GLN SER VAL ILE HIS SER MET VAL
SEQRES 21 B 398 ARG TYR GLN ASP GLY SER VAL LEU ALA GLN LEU GLY GLU
SEQRES 22 B 398 PRO ASP MET ARG THR PRO ILE ALA HIS THR MET ALA TRP
SEQRES 23 B 398 PRO ASN ARG VAL ASN SER GLY VAL LYS PRO LEU ASP PHE
SEQRES 24 B 398 CYS LYS LEU SER ALA LEU THR PHE ALA ALA PRO ASP TYR
SEQRES 25 B 398 ASP ARG TYR PRO CYS LEU LYS LEU ALA MET GLU ALA PHE
SEQRES 26 B 398 GLU GLN GLY GLN ALA ALA THR THR ALA LEU ASN ALA ALA
SEQRES 27 B 398 ASN GLU ILE THR VAL ALA ALA PHE LEU ALA GLN GLN ILE
SEQRES 28 B 398 ARG PHE THR ASP ILE ALA ALA LEU ASN LEU SER VAL LEU
SEQRES 29 B 398 GLU LYS MET ASP MET ARG GLU PRO GLN CYS VAL ASP ASP
SEQRES 30 B 398 VAL LEU SER VAL ASP ALA ASN ALA ARG GLU VAL ALA ARG
SEQRES 31 B 398 LYS GLU VAL MET ARG LEU ALA SER
FORMUL 3 HOH *316(H2 O)
HELIX 1 1 GLY A 11 HIS A 23 1 13
HELIX 2 2 ASN A 38 SER A 50 1 13
HELIX 3 3 ASP A 58 GLY A 73 1 16
HELIX 4 4 GLY A 81 ALA A 90 1 10
HELIX 5 5 GLY A 103 ALA A 105 5 3
HELIX 6 6 GLY A 106 ALA A 116 1 11
HELIX 7 7 LYS A 125 CYS A 131 1 7
HELIX 8 8 CYS A 131 LYS A 143 1 13
HELIX 9 9 ASP A 150 SER A 159 1 10
HELIX 10 10 PRO A 161 HIS A 166 1 6
HELIX 11 11 LEU A 173 ASN A 176 5 4
HELIX 12 12 ASP A 197 MET A 201 5 5
HELIX 13 13 THR A 202 CYS A 207 1 6
HELIX 14 14 ARG A 216 MET A 225 1 10
HELIX 15 15 MET A 225 PHE A 239 1 15
HELIX 16 16 SER A 242 SER A 244 5 3
HELIX 17 17 MET A 276 TRP A 286 1 11
HELIX 18 18 TYR A 315 GLY A 328 1 14
HELIX 19 19 GLY A 328 ALA A 348 1 21
HELIX 20 20 THR A 354 LYS A 366 1 13
HELIX 21 21 CYS A 374 ALA A 397 1 24
HELIX 22 22 GLY B 11 ASN B 24 1 14
HELIX 23 23 ASN B 38 PHE B 49 1 12
HELIX 24 24 ASP B 58 GLY B 73 1 16
HELIX 25 25 GLY B 81 ALA B 90 1 10
HELIX 26 26 GLY B 103 ALA B 105 5 3
HELIX 27 27 GLY B 106 ALA B 116 1 11
HELIX 28 28 LYS B 125 CYS B 131 1 7
HELIX 29 29 CYS B 131 LYS B 143 1 13
HELIX 30 30 ASP B 150 SER B 159 1 10
HELIX 31 31 PRO B 161 HIS B 166 1 6
HELIX 32 32 LEU B 173 ASN B 176 5 4
HELIX 33 33 THR B 202 CYS B 207 1 6
HELIX 34 34 ARG B 216 MET B 225 1 10
HELIX 35 35 MET B 225 PHE B 239 1 15
HELIX 36 36 SER B 242 SER B 244 5 3
HELIX 37 37 MET B 276 TRP B 286 1 11
HELIX 38 38 TYR B 315 GLY B 328 1 14
HELIX 39 39 GLY B 328 ALA B 348 1 21
HELIX 40 40 THR B 354 LYS B 366 1 13
HELIX 41 41 CYS B 374 ARG B 395 1 22
SHEET 1 A 7 GLU A 77 SER A 80 0
SHEET 2 A 7 TYR A 53 MET A 56 1 N ALA A 54 O LEU A 79
SHEET 3 A 7 PHE A 28 VAL A 34 1 N LEU A 33 O VAL A 55
SHEET 4 A 7 LYS A 2 LEU A 7 1 N LEU A 4 O VAL A 31
SHEET 5 A 7 GLN A 96 ALA A 99 1 O MET A 98 N LEU A 7
SHEET 6 A 7 THR A 119 LEU A 122 1 O THR A 119 N VAL A 97
SHEET 7 A 7 GLN A 145 PRO A 148 1 O GLN A 145 N ILE A 120
SHEET 1 B 8 MET A 246 ILE A 250 0
SHEET 2 B 8 VAL A 178 GLY A 185 1 N LEU A 183 O LEU A 249
SHEET 3 B 8 ILE A 256 TYR A 262 -1 O MET A 259 N LEU A 182
SHEET 4 B 8 VAL A 267 LEU A 271 -1 O LEU A 268 N VAL A 260
SHEET 5 B 8 VAL B 267 LEU B 271 -1 O VAL B 267 N LEU A 271
SHEET 6 B 8 ILE B 256 TYR B 262 -1 N VAL B 260 O LEU B 268
SHEET 7 B 8 VAL B 178 GLY B 185 -1 N LEU B 182 O MET B 259
SHEET 8 B 8 MET B 246 ILE B 250 1 O GLU B 247 N LEU B 183
SHEET 1 C 7 GLU B 77 SER B 80 0
SHEET 2 C 7 TYR B 53 MET B 56 1 N ALA B 54 O LEU B 79
SHEET 3 C 7 PHE B 28 VAL B 34 1 N LEU B 33 O VAL B 55
SHEET 4 C 7 LYS B 2 LEU B 7 1 N LEU B 4 O VAL B 31
SHEET 5 C 7 GLN B 96 ALA B 99 1 O MET B 98 N LEU B 7
SHEET 6 C 7 THR B 119 LEU B 122 1 O THR B 119 N VAL B 97
SHEET 7 C 7 GLN B 145 LEU B 146 1 O GLN B 145 N ILE B 120
CISPEP 1 TRP A 286 PRO A 287 0 0.40
CISPEP 2 TRP B 286 PRO B 287 0 1.37
CRYST1 90.396 53.419 107.490 90.00 92.85 90.00 P 1 21 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 0.011062 0.000000 0.000551 0.00000
SCALE2 0.000000 0.018720 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009315 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
