HEADER OXIDOREDUCTASE 18-JAN-06 2FR0
TITLE THE FIRST KETOREDUCTASE OF THE ERYTHROMYCIN SYNTHASE (CRYSTAL FORM 1)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ERYTHROMYCIN SYNTHASE, ERYAI;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: RESIDUES 1444-1925;
COMPND 5 EC: 1.1.1.100;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SACCHAROPOLYSPORA ERYTHRAEA;
SOURCE 3 ORGANISM_TAXID: 1836;
SOURCE 4 GENE: ERYAI;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET28B
KEYWDS SHORT CHAIN DEHYDROGENASE/REDUCTASE, OXIDOREDUCTASE
EXPDTA X-RAY DIFFRACTION
AUTHOR A.T.KEATINGE-CLAY,R.M.STROUD
REVDAT 5 03-APR-24 2FR0 1 REMARK
REVDAT 4 14-FEB-24 2FR0 1 REMARK SEQADV
REVDAT 3 24-FEB-09 2FR0 1 VERSN
REVDAT 2 02-MAY-06 2FR0 1 JRNL
REVDAT 1 04-APR-06 2FR0 0
JRNL AUTH A.T.KEATINGE-CLAY,R.M.STROUD
JRNL TITL THE STRUCTURE OF A KETOREDUCTASE DETERMINES THE ORGANIZATION
JRNL TITL 2 OF THE BETA-CARBON PROCESSING ENZYMES OF MODULAR POLYKETIDE
JRNL TITL 3 SYNTHASES
JRNL REF STRUCTURE V. 14 737 2006
JRNL REFN ISSN 0969-2126
JRNL PMID 16564177
JRNL DOI 10.1016/J.STR.2006.01.009
REMARK 2
REMARK 2 RESOLUTION. 1.81 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) : 1.81
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 45.60
REMARK 3 DATA CUTOFF (SIGMA(F)) : 2.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 93.7
REMARK 3 NUMBER OF REFLECTIONS : 40140
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) : 0.235
REMARK 3 FREE R VALUE : 0.263
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : 4014
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 : 3468
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 48
REMARK 3 SOLVENT ATOMS : 180
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) : 0.007
REMARK 3 BOND ANGLES (DEGREES) : 1.200
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 : PROTEIN_REP.PARAM
REMARK 3 PARAMETER FILE 2 : WATER_REP.PARAM
REMARK 3 PARAMETER FILE 3 : NADPH.PARAM
REMARK 3 PARAMETER FILE 4 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3 TOPOLOGY FILE 2 : NULL
REMARK 3 TOPOLOGY FILE 3 : NULL
REMARK 3 TOPOLOGY FILE 4 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2FR0 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 09-JAN-06.
REMARK 100 THE DEPOSITION ID IS D_1000036207.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 28-MAY-05
REMARK 200 TEMPERATURE (KELVIN) : 200
REMARK 200 PH : 7.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ALS
REMARK 200 BEAMLINE : 8.3.1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.1158
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 4
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 40140
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.810
REMARK 200 RESOLUTION RANGE LOW (A) : 45.600
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 93.7
REMARK 200 DATA REDUNDANCY : 1.800
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.05800
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 8.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.81
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.89
REMARK 200 COMPLETENESS FOR SHELL (%) : 80.9
REMARK 200 DATA REDUNDANCY IN SHELL : 1.60
REMARK 200 R MERGE FOR SHELL (I) : 0.30200
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.000
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD
REMARK 200 SOFTWARE USED: CNS
REMARK 200 STARTING MODEL: AB INITIO
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 48.15
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.37
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.5 MG/ML PROTEIN, 5.05 MM HEPES, 75
REMARK 280 MM NACL, 0.5 MM DTT, 17.5% PEG3350, 0.1 M GUANIDINIUM
REMARK 280 HYDROCHLORIDE, PH 7.0, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 295K
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: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
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 GLY A 1440
REMARK 465 SER A 1441
REMARK 465 HIS A 1442
REMARK 465 MET A 1443
REMARK 465 SER A 1444
REMARK 465 THR A 1445
REMARK 465 GLU A 1446
REMARK 465 VAL A 1447
REMARK 465 ALA A 1916
REMARK 465 ALA A 1917
REMARK 465 PRO A 1918
REMARK 465 GLN A 1919
REMARK 465 ALA A 1920
REMARK 465 ALA A 1921
REMARK 465 ALA A 1922
REMARK 465 GLU A 1923
REMARK 465 PRO A 1924
REMARK 465 ARG A 1925
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 A1464 -80.66 -88.72
REMARK 500 GLU A1466 99.15 58.77
REMARK 500 ARG A1469 -166.11 46.02
REMARK 500 LEU A1470 -163.24 -115.84
REMARK 500 ASP A1471 106.03 177.18
REMARK 500 PRO A1539 -159.23 -65.29
REMARK 500 GLU A1540 -145.88 -73.48
REMARK 500 GLU A1541 -176.37 62.71
REMARK 500 ALA A1654 -140.42 -76.98
REMARK 500 ASP A1758 118.85 69.22
REMARK 500 GLU A1849 144.35 70.93
REMARK 500 GLN A1901 16.73 -144.39
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 NDP A 201
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2FR1 RELATED DB: PDB
REMARK 900 THE FIRST KETOREDUCTASE OF THE ERYTHROMYCIN SYNTHASE (CRYSTAL FORM
REMARK 900 2)
REMARK 900 RELATED ID: 2FRO RELATED DB: PDB
REMARK 900 MODEL OF THE BETA-CARBON PROCESSING ENZYMES AND ACYL CARRIER
REMARK 900 PROTEIN OF MODULAR POLYKETIDE SYNTHASES
DBREF 2FR0 A 1444 1925 UNP Q03131 ERYA1_SACER 1391 1872
SEQADV 2FR0 GLY A 1440 UNP Q03131 CLONING ARTIFACT
SEQADV 2FR0 SER A 1441 UNP Q03131 CLONING ARTIFACT
SEQADV 2FR0 HIS A 1442 UNP Q03131 CLONING ARTIFACT
SEQADV 2FR0 MET A 1443 UNP Q03131 CLONING ARTIFACT
SEQRES 1 A 486 GLY SER HIS MET SER THR GLU VAL ASP GLU VAL SER ALA
SEQRES 2 A 486 LEU ARG TYR ARG ILE GLU TRP ARG PRO THR GLY ALA GLY
SEQRES 3 A 486 GLU PRO ALA ARG LEU ASP GLY THR TRP LEU VAL ALA LYS
SEQRES 4 A 486 TYR ALA GLY THR ALA ASP GLU THR SER THR ALA ALA ARG
SEQRES 5 A 486 GLU ALA LEU GLU SER ALA GLY ALA ARG VAL ARG GLU LEU
SEQRES 6 A 486 VAL VAL ASP ALA ARG CYS GLY ARG ASP GLU LEU ALA GLU
SEQRES 7 A 486 ARG LEU ARG SER VAL GLY GLU VAL ALA GLY VAL LEU SER
SEQRES 8 A 486 LEU LEU ALA VAL ASP GLU ALA GLU PRO GLU GLU ALA PRO
SEQRES 9 A 486 LEU ALA LEU ALA SER LEU ALA ASP THR LEU SER LEU VAL
SEQRES 10 A 486 GLN ALA MET VAL SER ALA GLU LEU GLY CYS PRO LEU TRP
SEQRES 11 A 486 THR VAL THR GLU SER ALA VAL ALA THR GLY PRO PHE GLU
SEQRES 12 A 486 ARG VAL ARG ASN ALA ALA HIS GLY ALA LEU TRP GLY VAL
SEQRES 13 A 486 GLY ARG VAL ILE ALA LEU GLU ASN PRO ALA VAL TRP GLY
SEQRES 14 A 486 GLY LEU VAL ASP VAL PRO ALA GLY SER VAL ALA GLU LEU
SEQRES 15 A 486 ALA ARG HIS LEU ALA ALA VAL VAL SER GLY GLY ALA GLY
SEQRES 16 A 486 GLU ASP GLN LEU ALA LEU ARG ALA ASP GLY VAL TYR GLY
SEQRES 17 A 486 ARG ARG TRP VAL ARG ALA ALA ALA PRO ALA THR ASP ASP
SEQRES 18 A 486 GLU TRP LYS PRO THR GLY THR VAL LEU VAL THR GLY GLY
SEQRES 19 A 486 THR GLY GLY VAL GLY GLY GLN ILE ALA ARG TRP LEU ALA
SEQRES 20 A 486 ARG ARG GLY ALA PRO HIS LEU LEU LEU VAL SER ARG SER
SEQRES 21 A 486 GLY PRO ASP ALA ASP GLY ALA GLY GLU LEU VAL ALA GLU
SEQRES 22 A 486 LEU GLU ALA LEU GLY ALA ARG THR THR VAL ALA ALA CYS
SEQRES 23 A 486 ASP VAL THR ASP ARG GLU SER VAL ARG GLU LEU LEU GLY
SEQRES 24 A 486 GLY ILE GLY ASP ASP VAL PRO LEU SER ALA VAL PHE HIS
SEQRES 25 A 486 ALA ALA ALA THR LEU ASP ASP GLY THR VAL ASP THR LEU
SEQRES 26 A 486 THR GLY GLU ARG ILE GLU ARG ALA SER ARG ALA LYS VAL
SEQRES 27 A 486 LEU GLY ALA ARG ASN LEU HIS GLU LEU THR ARG GLU LEU
SEQRES 28 A 486 ASP LEU THR ALA PHE VAL LEU PHE SER SER PHE ALA SER
SEQRES 29 A 486 ALA PHE GLY ALA PRO GLY LEU GLY GLY TYR ALA PRO GLY
SEQRES 30 A 486 ASN ALA TYR LEU ASP GLY LEU ALA GLN GLN ARG ARG SER
SEQRES 31 A 486 ASP GLY LEU PRO ALA THR ALA VAL ALA TRP GLY THR TRP
SEQRES 32 A 486 ALA GLY SER GLY MET ALA GLU GLY PRO VAL ALA ASP ARG
SEQRES 33 A 486 PHE ARG ARG HIS GLY VAL ILE GLU MET PRO PRO GLU THR
SEQRES 34 A 486 ALA CYS ARG ALA LEU GLN ASN ALA LEU ASP ARG ALA GLU
SEQRES 35 A 486 VAL CYS PRO ILE VAL ILE ASP VAL ARG TRP ASP ARG PHE
SEQRES 36 A 486 LEU LEU ALA TYR THR ALA GLN ARG PRO THR ARG LEU PHE
SEQRES 37 A 486 ASP GLU ILE ASP ASP ALA ARG ARG ALA ALA PRO GLN ALA
SEQRES 38 A 486 ALA ALA GLU PRO ARG
HET NDP A 201 48
HETNAM NDP NADPH DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE
HETNAM 2 NDP PHOSPHATE
FORMUL 2 NDP C21 H30 N7 O17 P3
FORMUL 3 HOH *180(H2 O)
HELIX 1 1 ALA A 1483 SER A 1496 1 14
HELIX 2 2 GLY A 1511 ARG A 1520 1 10
HELIX 3 3 ALA A 1542 ALA A 1545 5 4
HELIX 4 4 LEU A 1546 GLU A 1563 1 18
HELIX 5 5 ASN A 1586 ALA A 1588 5 3
HELIX 6 6 HIS A 1589 ASN A 1603 1 15
HELIX 7 7 VAL A 1618 SER A 1630 1 13
HELIX 8 8 GLY A 1675 GLY A 1689 1 15
HELIX 9 9 SER A 1699 ALA A 1703 5 5
HELIX 10 10 GLY A 1705 ALA A 1715 1 11
HELIX 11 11 ASP A 1729 GLY A 1738 1 10
HELIX 12 12 THR A 1760 LEU A 1764 5 5
HELIX 13 13 THR A 1765 SER A 1773 1 9
HELIX 14 14 SER A 1773 ARG A 1788 1 16
HELIX 15 15 PHE A 1801 PHE A 1805 1 5
HELIX 16 16 TYR A 1813 ASP A 1830 1 18
HELIX 17 17 PRO A 1851 ARG A 1858 1 8
HELIX 18 18 PRO A 1865 ARG A 1879 1 15
HELIX 19 19 ARG A 1890 THR A 1899 1 10
HELIX 20 20 ILE A 1910 ARG A 1915 1 6
SHEET 1 A15 ARG A1500 VAL A1506 0
SHEET 2 A15 THR A1473 TYR A1479 1 N TRP A1474 O ARG A1502
SHEET 3 A15 GLY A1527 SER A1530 1 O LEU A1529 N LEU A1475
SHEET 4 A15 LEU A1568 GLU A1573 1 O TRP A1569 N SER A1530
SHEET 5 A15 TRP A1607 VAL A1613 1 O VAL A1611 N THR A1570
SHEET 6 A15 GLN A1637 ARG A1641 1 O LEU A1640 N ASP A1612
SHEET 7 A15 GLY A1644 ARG A1652 -1 O TYR A1646 N ALA A1639
SHEET 8 A15 ARG A1454 PRO A1461 -1 N GLU A1458 O ARG A1649
SHEET 9 A15 ILE A1885 VAL A1886 -1 O ILE A1885 N TYR A1455
SHEET 10 A15 THR A1835 TRP A1839 1 N ALA A1838 O VAL A1886
SHEET 11 A15 ALA A1794 SER A1800 1 N LEU A1797 O THR A1835
SHEET 12 A15 LEU A1746 HIS A1751 1 N VAL A1749 O VAL A1796
SHEET 13 A15 THR A1667 THR A1671 1 N LEU A1669 O ALA A1748
SHEET 14 A15 HIS A1692 SER A1697 1 O LEU A1694 N VAL A1670
SHEET 15 A15 ARG A1719 ALA A1724 1 O THR A1721 N LEU A1695
SHEET 1 B 2 VAL A1861 ILE A1862 0
SHEET 2 B 2 ASP A1888 VAL A1889 -1 O ASP A1888 N ILE A1862
SITE 1 AC1 27 HOH A 53 HOH A 62 HOH A 126 GLY A1672
SITE 2 AC1 27 THR A1674 GLY A1675 GLY A1676 VAL A1677
SITE 3 AC1 27 SER A1697 ARG A1698 SER A1699 GLY A1700
SITE 4 AC1 27 ALA A1703 CYS A1725 ASP A1726 VAL A1727
SITE 5 AC1 27 THR A1728 ALA A1752 ALA A1753 ALA A1754
SITE 6 AC1 27 ALA A1775 LYS A1776 PHE A1798 SER A1799
SITE 7 AC1 27 PHE A1801 TYR A1813 MET A1847
CRYST1 43.211 46.332 61.506 94.73 90.17 98.89 P 1 1
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 0.023142 0.003620 0.000374 0.00000
SCALE2 0.000000 0.021846 0.001840 0.00000
SCALE3 0.000000 0.000000 0.016316 0.00000
(ATOM LINES ARE NOT SHOWN.)
END