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HEADER HYDROLASE 26-JUN-24 9CEL
TITLE JUVENIMICIN THIOESTERASE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TYPE I PKS MODULE 7;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MICROMONOSPORA CHALCEA SUBSP. IZUMENSIS;
SOURCE 3 ORGANISM_TAXID: 2008351;
SOURCE 4 GENE: JUVEV;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS THIOESTERASE, BIOSYNTHESIS, NATURAL PRODUCTS, PKS, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR D.L.AKEY,J.S.SMITH,V.CHOUDHARY
REVDAT 1 18-SEP-24 9CEL 0
JRNL AUTH T.M.MCCULLOUGH,V.CHOUDHARY,D.L.AKEY,M.A.SKIBA,S.M.BERNARD,
JRNL AUTH 2 J.D.KITTENDORF,J.J.SCHMIDT,D.H.SHERMAN,J.L.SMITH
JRNL TITL SUBSTRATE TRAPPING IN POLYKETIDE SYNTHASE THIOESTERASE
JRNL TITL 2 DOMAINS: STRUCTURAL BASIS FOR MACROLACTONE FORMATION
JRNL REF ACS CATALYSIS V. 14 2024
JRNL REFN ESSN 2155-5435
JRNL DOI 10.1021/ACSCATAL.4C03637
REMARK 2
REMARK 2 RESOLUTION. 2.27 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.21_5207
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : GEOSTD + MONOMER LIBRARY + CDL V1.2
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.27
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 45.62
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.120
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.8
REMARK 3 NUMBER OF REFLECTIONS : 44971
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.204
REMARK 3 R VALUE (WORKING SET) : 0.201
REMARK 3 FREE R VALUE : 0.262
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.550
REMARK 3 FREE R VALUE TEST SET COUNT : 2047
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 45.6200 - 5.5900 0.97 2912 143 0.1781 0.2403
REMARK 3 2 5.5900 - 4.4400 0.98 2900 136 0.1644 0.1958
REMARK 3 3 4.4400 - 3.8800 0.98 2871 138 0.1701 0.2076
REMARK 3 4 3.8800 - 3.5200 0.98 2861 133 0.1947 0.2499
REMARK 3 5 3.5200 - 3.2700 0.98 2881 142 0.2089 0.2772
REMARK 3 6 3.2700 - 3.0800 0.99 2890 147 0.2157 0.3330
REMARK 3 7 3.0800 - 2.9200 0.99 2919 126 0.2386 0.3214
REMARK 3 8 2.9200 - 2.8000 0.99 2874 142 0.2306 0.2800
REMARK 3 9 2.8000 - 2.6900 0.99 2885 137 0.2289 0.3055
REMARK 3 10 2.6900 - 2.5900 0.98 2871 128 0.2202 0.3286
REMARK 3 11 2.5900 - 2.5100 0.99 2868 145 0.2364 0.2805
REMARK 3 12 2.5100 - 2.4400 0.99 2832 144 0.2384 0.3342
REMARK 3 13 2.4400 - 2.3800 0.99 2937 133 0.2626 0.3361
REMARK 3 14 2.3800 - 2.3200 0.99 2898 133 0.2677 0.3520
REMARK 3 15 2.3200 - 2.2700 0.88 2525 120 0.2879 0.3720
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.10
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.356
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 30.475
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 45.73
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 54.05
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 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.008 7639
REMARK 3 ANGLE : 0.925 10465
REMARK 3 CHIRALITY : 0.049 1209
REMARK 3 PLANARITY : 0.010 1374
REMARK 3 DIHEDRAL : 15.639 2654
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 9CEL COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 27-JUN-24.
REMARK 100 THE DEPOSITION ID IS D_1000285312.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 14-JUL-19
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 23-ID-D
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.033
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS3 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XDS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 44988
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.260
REMARK 200 RESOLUTION RANGE LOW (A) : 45.620
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 94.4
REMARK 200 DATA REDUNDANCY : 3.300
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 7.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.27
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.29
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
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 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: PHENIX
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 44.30
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.21
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 20 MM MGCL2, 22% (W/V) POLYACRYLIC
REMARK 280 ACID 5100, 100 MM HEPES PH 7.5, VAPOR DIFFUSION, SITTING DROP,
REMARK 280 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 47.83300
REMARK 290 SMTRY3 2 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: 1530 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 21720 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -9.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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 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: 1490 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 21940 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -10.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, 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 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 1672
REMARK 465 ALA A 1673
REMARK 465 MET A 1674
REMARK 465 GLY A 1675
REMARK 465 VAL A 1676
REMARK 465 TRP A 1677
REMARK 465 ARG A 1678
REMARK 465 GLU A 1679
REMARK 465 GLU A 1680
REMARK 465 MET A 1681
REMARK 465 LEU A 1682
REMARK 465 ALA A 1683
REMARK 465 TRP A 1684
REMARK 465 VAL A 1685
REMARK 465 ALA A 1686
REMARK 465 GLU A 1687
REMARK 465 ARG A 1688
REMARK 465 SER A 1689
REMARK 465 VAL A 1690
REMARK 465 TRP A 1732
REMARK 465 PRO A 1733
REMARK 465 ASP A 1734
REMARK 465 PRO A 1735
REMARK 465 ARG A 1736
REMARK 465 GLN A 1737
REMARK 465 GLY B 1672
REMARK 465 ALA B 1673
REMARK 465 MET B 1674
REMARK 465 GLY B 1675
REMARK 465 VAL B 1676
REMARK 465 TRP B 1677
REMARK 465 ARG B 1678
REMARK 465 GLU B 1679
REMARK 465 GLU B 1680
REMARK 465 MET B 1681
REMARK 465 LEU B 1682
REMARK 465 ALA B 1683
REMARK 465 TRP B 1684
REMARK 465 VAL B 1685
REMARK 465 ALA B 1686
REMARK 465 GLU B 1687
REMARK 465 ARG B 1688
REMARK 465 SER B 1689
REMARK 465 VAL B 1690
REMARK 465 VAL B 1691
REMARK 465 PRO B 1733
REMARK 465 ALA C 1670
REMARK 465 PRO C 1671
REMARK 465 GLY C 1672
REMARK 465 ALA C 1673
REMARK 465 MET C 1674
REMARK 465 ARG C 1688
REMARK 465 SER C 1689
REMARK 465 VAL C 1690
REMARK 465 TRP C 1732
REMARK 465 PRO C 1733
REMARK 465 ASP C 1734
REMARK 465 PRO C 1735
REMARK 465 ARG C 1736
REMARK 465 GLN C 1737
REMARK 465 ALA D 1670
REMARK 465 PRO D 1671
REMARK 465 GLY D 1672
REMARK 465 ALA D 1673
REMARK 465 MET D 1674
REMARK 465 GLU D 1687
REMARK 465 ARG D 1688
REMARK 465 SER D 1689
REMARK 465 VAL D 1690
REMARK 465 GLN D 1737
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 O PRO B 1715 O HOH B 1801 2.08
REMARK 500 NE ARG C 1697 O HOH C 1801 2.18
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 THR A1536 1.14 -66.54
REMARK 500 ALA A1574 46.18 -78.44
REMARK 500 ALA A1627 51.07 33.78
REMARK 500 SER A1637 -113.71 39.89
REMARK 500 ARG A1714 142.27 -37.99
REMARK 500 THR A1761 -87.18 -119.17
REMARK 500 ASP A1776 1.60 -63.17
REMARK 500 SER B1637 -135.09 54.76
REMARK 500 ARG B1714 155.20 -43.58
REMARK 500 PHE B1743 107.92 -161.28
REMARK 500 THR B1761 -93.02 -117.32
REMARK 500 SER C1637 -120.22 34.90
REMARK 500 THR C1761 -86.95 -123.68
REMARK 500 ALA D1574 42.29 -92.93
REMARK 500 SER D1637 -133.80 54.93
REMARK 500 PRO D1668 39.46 -63.76
REMARK 500 THR D1761 -89.71 -118.84
REMARK 500
REMARK 500 REMARK: NULL
DBREF1 9CEL A 1508 1778 UNP A0A1Z1MZ81_MICCH
DBREF2 9CEL A A0A1Z1MZ81 1508 1778
DBREF1 9CEL B 1508 1778 UNP A0A1Z1MZ81_MICCH
DBREF2 9CEL B A0A1Z1MZ81 1508 1778
DBREF1 9CEL C 1508 1778 UNP A0A1Z1MZ81_MICCH
DBREF2 9CEL C A0A1Z1MZ81 1508 1778
DBREF1 9CEL D 1508 1778 UNP A0A1Z1MZ81_MICCH
DBREF2 9CEL D A0A1Z1MZ81 1508 1778
SEQRES 1 A 271 GLY SER ALA LEU VAL GLU MET TYR ARG ARG ALA VAL ALA
SEQRES 2 A 271 THR GLY ARG ALA ALA GLU ALA VAL GLU VAL LEU GLY THR
SEQRES 3 A 271 VAL ALA THR PHE ARG PRO VAL PHE ARG SER PRO ASP GLU
SEQRES 4 A 271 LEU GLY GLU PRO PRO ALA LEU VAL PRO LEU GLY THR GLY
SEQRES 5 A 271 ALA GLY GLY PRO THR LEU VAL CYS CYS ALA GLY THR ALA
SEQRES 6 A 271 ALA ALA SER GLY PRO ARG GLU PHE THR ALA PHE ALA ALA
SEQRES 7 A 271 ALA LEU ALA GLY LEU ARG ASP VAL THR VAL LEU PRO GLN
SEQRES 8 A 271 THR GLY PHE LEU THR GLY GLU PRO LEU PRO ALA GLY LEU
SEQRES 9 A 271 ASP VAL LEU LEU ASP ALA GLN ALA ASP ALA VAL LEU ALA
SEQRES 10 A 271 HIS CYS ALA GLY ARG PRO PHE VAL LEU VAL GLY HIS SER
SEQRES 11 A 271 ALA GLY ALA ASN MET ALA HIS ALA LEU THR VAL ARG LEU
SEQRES 12 A 271 GLU ALA ARG GLY ALA ASP PRO ALA ALA LEU VAL LEU MET
SEQRES 13 A 271 ASP ILE TYR THR PRO ALA ALA PRO GLY ALA MET GLY VAL
SEQRES 14 A 271 TRP ARG GLU GLU MET LEU ALA TRP VAL ALA GLU ARG SER
SEQRES 15 A 271 VAL VAL PRO VAL ASP ASP THR ARG LEU THR ALA MET GLY
SEQRES 16 A 271 ALA TYR HIS ARG LEU LEU LEU ASP TRP ALA PRO ARG PRO
SEQRES 17 A 271 THR ARG ALA PRO VAL LEU HIS LEU TYR ALA GLY GLU PRO
SEQRES 18 A 271 ALA GLY ALA TRP PRO ASP PRO ARG GLN ASP TRP ARG SER
SEQRES 19 A 271 ARG PHE ASP GLY ALA HIS THR SER ALA GLU VAL PRO GLY
SEQRES 20 A 271 THR HIS PHE SER MET MET THR GLU HIS ALA PRO VAL THR
SEQRES 21 A 271 ALA ALA THR VAL HIS LYS TRP LEU ASP GLU VAL
SEQRES 1 B 271 GLY SER ALA LEU VAL GLU MET TYR ARG ARG ALA VAL ALA
SEQRES 2 B 271 THR GLY ARG ALA ALA GLU ALA VAL GLU VAL LEU GLY THR
SEQRES 3 B 271 VAL ALA THR PHE ARG PRO VAL PHE ARG SER PRO ASP GLU
SEQRES 4 B 271 LEU GLY GLU PRO PRO ALA LEU VAL PRO LEU GLY THR GLY
SEQRES 5 B 271 ALA GLY GLY PRO THR LEU VAL CYS CYS ALA GLY THR ALA
SEQRES 6 B 271 ALA ALA SER GLY PRO ARG GLU PHE THR ALA PHE ALA ALA
SEQRES 7 B 271 ALA LEU ALA GLY LEU ARG ASP VAL THR VAL LEU PRO GLN
SEQRES 8 B 271 THR GLY PHE LEU THR GLY GLU PRO LEU PRO ALA GLY LEU
SEQRES 9 B 271 ASP VAL LEU LEU ASP ALA GLN ALA ASP ALA VAL LEU ALA
SEQRES 10 B 271 HIS CYS ALA GLY ARG PRO PHE VAL LEU VAL GLY HIS SER
SEQRES 11 B 271 ALA GLY ALA ASN MET ALA HIS ALA LEU THR VAL ARG LEU
SEQRES 12 B 271 GLU ALA ARG GLY ALA ASP PRO ALA ALA LEU VAL LEU MET
SEQRES 13 B 271 ASP ILE TYR THR PRO ALA ALA PRO GLY ALA MET GLY VAL
SEQRES 14 B 271 TRP ARG GLU GLU MET LEU ALA TRP VAL ALA GLU ARG SER
SEQRES 15 B 271 VAL VAL PRO VAL ASP ASP THR ARG LEU THR ALA MET GLY
SEQRES 16 B 271 ALA TYR HIS ARG LEU LEU LEU ASP TRP ALA PRO ARG PRO
SEQRES 17 B 271 THR ARG ALA PRO VAL LEU HIS LEU TYR ALA GLY GLU PRO
SEQRES 18 B 271 ALA GLY ALA TRP PRO ASP PRO ARG GLN ASP TRP ARG SER
SEQRES 19 B 271 ARG PHE ASP GLY ALA HIS THR SER ALA GLU VAL PRO GLY
SEQRES 20 B 271 THR HIS PHE SER MET MET THR GLU HIS ALA PRO VAL THR
SEQRES 21 B 271 ALA ALA THR VAL HIS LYS TRP LEU ASP GLU VAL
SEQRES 1 C 271 GLY SER ALA LEU VAL GLU MET TYR ARG ARG ALA VAL ALA
SEQRES 2 C 271 THR GLY ARG ALA ALA GLU ALA VAL GLU VAL LEU GLY THR
SEQRES 3 C 271 VAL ALA THR PHE ARG PRO VAL PHE ARG SER PRO ASP GLU
SEQRES 4 C 271 LEU GLY GLU PRO PRO ALA LEU VAL PRO LEU GLY THR GLY
SEQRES 5 C 271 ALA GLY GLY PRO THR LEU VAL CYS CYS ALA GLY THR ALA
SEQRES 6 C 271 ALA ALA SER GLY PRO ARG GLU PHE THR ALA PHE ALA ALA
SEQRES 7 C 271 ALA LEU ALA GLY LEU ARG ASP VAL THR VAL LEU PRO GLN
SEQRES 8 C 271 THR GLY PHE LEU THR GLY GLU PRO LEU PRO ALA GLY LEU
SEQRES 9 C 271 ASP VAL LEU LEU ASP ALA GLN ALA ASP ALA VAL LEU ALA
SEQRES 10 C 271 HIS CYS ALA GLY ARG PRO PHE VAL LEU VAL GLY HIS SER
SEQRES 11 C 271 ALA GLY ALA ASN MET ALA HIS ALA LEU THR VAL ARG LEU
SEQRES 12 C 271 GLU ALA ARG GLY ALA ASP PRO ALA ALA LEU VAL LEU MET
SEQRES 13 C 271 ASP ILE TYR THR PRO ALA ALA PRO GLY ALA MET GLY VAL
SEQRES 14 C 271 TRP ARG GLU GLU MET LEU ALA TRP VAL ALA GLU ARG SER
SEQRES 15 C 271 VAL VAL PRO VAL ASP ASP THR ARG LEU THR ALA MET GLY
SEQRES 16 C 271 ALA TYR HIS ARG LEU LEU LEU ASP TRP ALA PRO ARG PRO
SEQRES 17 C 271 THR ARG ALA PRO VAL LEU HIS LEU TYR ALA GLY GLU PRO
SEQRES 18 C 271 ALA GLY ALA TRP PRO ASP PRO ARG GLN ASP TRP ARG SER
SEQRES 19 C 271 ARG PHE ASP GLY ALA HIS THR SER ALA GLU VAL PRO GLY
SEQRES 20 C 271 THR HIS PHE SER MET MET THR GLU HIS ALA PRO VAL THR
SEQRES 21 C 271 ALA ALA THR VAL HIS LYS TRP LEU ASP GLU VAL
SEQRES 1 D 271 GLY SER ALA LEU VAL GLU MET TYR ARG ARG ALA VAL ALA
SEQRES 2 D 271 THR GLY ARG ALA ALA GLU ALA VAL GLU VAL LEU GLY THR
SEQRES 3 D 271 VAL ALA THR PHE ARG PRO VAL PHE ARG SER PRO ASP GLU
SEQRES 4 D 271 LEU GLY GLU PRO PRO ALA LEU VAL PRO LEU GLY THR GLY
SEQRES 5 D 271 ALA GLY GLY PRO THR LEU VAL CYS CYS ALA GLY THR ALA
SEQRES 6 D 271 ALA ALA SER GLY PRO ARG GLU PHE THR ALA PHE ALA ALA
SEQRES 7 D 271 ALA LEU ALA GLY LEU ARG ASP VAL THR VAL LEU PRO GLN
SEQRES 8 D 271 THR GLY PHE LEU THR GLY GLU PRO LEU PRO ALA GLY LEU
SEQRES 9 D 271 ASP VAL LEU LEU ASP ALA GLN ALA ASP ALA VAL LEU ALA
SEQRES 10 D 271 HIS CYS ALA GLY ARG PRO PHE VAL LEU VAL GLY HIS SER
SEQRES 11 D 271 ALA GLY ALA ASN MET ALA HIS ALA LEU THR VAL ARG LEU
SEQRES 12 D 271 GLU ALA ARG GLY ALA ASP PRO ALA ALA LEU VAL LEU MET
SEQRES 13 D 271 ASP ILE TYR THR PRO ALA ALA PRO GLY ALA MET GLY VAL
SEQRES 14 D 271 TRP ARG GLU GLU MET LEU ALA TRP VAL ALA GLU ARG SER
SEQRES 15 D 271 VAL VAL PRO VAL ASP ASP THR ARG LEU THR ALA MET GLY
SEQRES 16 D 271 ALA TYR HIS ARG LEU LEU LEU ASP TRP ALA PRO ARG PRO
SEQRES 17 D 271 THR ARG ALA PRO VAL LEU HIS LEU TYR ALA GLY GLU PRO
SEQRES 18 D 271 ALA GLY ALA TRP PRO ASP PRO ARG GLN ASP TRP ARG SER
SEQRES 19 D 271 ARG PHE ASP GLY ALA HIS THR SER ALA GLU VAL PRO GLY
SEQRES 20 D 271 THR HIS PHE SER MET MET THR GLU HIS ALA PRO VAL THR
SEQRES 21 D 271 ALA ALA THR VAL HIS LYS TRP LEU ASP GLU VAL
FORMUL 5 HOH *252(H2 O)
HELIX 1 AA1 SER A 1509 ALA A 1520 1 12
HELIX 2 AA2 ARG A 1523 THR A 1536 1 14
HELIX 3 AA3 SER A 1543 LEU A 1547 5 5
HELIX 4 AA4 GLY A 1576 GLU A 1579 5 4
HELIX 5 AA5 PHE A 1580 ALA A 1588 1 9
HELIX 6 AA6 GLY A 1610 CYS A 1626 1 17
HELIX 7 AA7 SER A 1637 ARG A 1653 1 17
HELIX 8 AA8 ASP A 1694 LEU A 1709 1 16
HELIX 9 AA9 PHE A 1757 THR A 1761 5 5
HELIX 10 AB1 HIS A 1763 ASP A 1776 1 14
HELIX 11 AB2 SER B 1509 THR B 1521 1 13
HELIX 12 AB3 ARG B 1523 THR B 1536 1 14
HELIX 13 AB4 PRO B 1544 GLY B 1548 5 5
HELIX 14 AB5 GLY B 1576 GLU B 1579 5 4
HELIX 15 AB6 PHE B 1580 ALA B 1588 1 9
HELIX 16 AB7 GLY B 1610 ALA B 1627 1 18
HELIX 17 AB8 SER B 1637 ARG B 1653 1 17
HELIX 18 AB9 ASP B 1694 LEU B 1708 1 15
HELIX 19 AC1 PHE B 1757 THR B 1761 5 5
HELIX 20 AC2 HIS B 1763 VAL B 1778 1 16
HELIX 21 AC3 SER C 1509 THR C 1521 1 13
HELIX 22 AC4 ARG C 1523 THR C 1536 1 14
HELIX 23 AC5 SER C 1543 GLY C 1548 5 6
HELIX 24 AC6 GLY C 1576 GLU C 1579 5 4
HELIX 25 AC7 PHE C 1580 LEU C 1587 1 8
HELIX 26 AC8 GLY C 1610 ALA C 1627 1 18
HELIX 27 AC9 SER C 1637 ARG C 1653 1 17
HELIX 28 AD1 VAL C 1676 ALA C 1686 1 11
HELIX 29 AD2 ASP C 1694 LEU C 1709 1 16
HELIX 30 AD3 PHE C 1757 THR C 1761 5 5
HELIX 31 AD4 HIS C 1763 ASP C 1776 1 14
HELIX 32 AD5 SER D 1509 THR D 1521 1 13
HELIX 33 AD6 ARG D 1523 THR D 1536 1 14
HELIX 34 AD7 GLY D 1576 GLU D 1579 5 4
HELIX 35 AD8 PHE D 1580 LEU D 1587 1 8
HELIX 36 AD9 GLY D 1610 ALA D 1627 1 18
HELIX 37 AE1 SER D 1637 ARG D 1653 1 17
HELIX 38 AE2 VAL D 1676 ALA D 1686 1 11
HELIX 39 AE3 ASP D 1694 LEU D 1708 1 15
HELIX 40 AE4 LEU D 1709 TRP D 1711 5 3
HELIX 41 AE5 PHE D 1757 THR D 1761 5 5
HELIX 42 AE6 HIS D 1763 GLU D 1777 1 15
SHEET 1 AA1 2 VAL A1540 PHE A1541 0
SHEET 2 AA1 2 LEU A1607 PRO A1608 1 O LEU A1607 N PHE A1541
SHEET 1 AA2 7 VAL A1554 GLY A1557 0
SHEET 2 AA2 7 ASP A1592 LEU A1596 -1 O VAL A1595 N VAL A1554
SHEET 3 AA2 7 THR A1564 CYS A1568 1 N CYS A1567 O THR A1594
SHEET 4 AA2 7 PHE A1631 HIS A1636 1 O VAL A1632 N VAL A1566
SHEET 5 AA2 7 ALA A1659 MET A1663 1 O VAL A1661 N LEU A1633
SHEET 6 AA2 7 VAL A1720 ALA A1725 1 O LEU A1721 N LEU A1662
SHEET 7 AA2 7 THR A1748 VAL A1752 1 O THR A1748 N HIS A1722
SHEET 1 AA3 2 VAL B1540 PHE B1541 0
SHEET 2 AA3 2 LEU B1607 PRO B1608 1 O LEU B1607 N PHE B1541
SHEET 1 AA4 7 VAL B1554 GLY B1557 0
SHEET 2 AA4 7 VAL B1593 LEU B1596 -1 O VAL B1595 N VAL B1554
SHEET 3 AA4 7 THR B1564 CYS B1568 1 N CYS B1567 O THR B1594
SHEET 4 AA4 7 PHE B1631 HIS B1636 1 O VAL B1632 N VAL B1566
SHEET 5 AA4 7 ALA B1659 MET B1663 1 O VAL B1661 N LEU B1633
SHEET 6 AA4 7 VAL B1720 ALA B1725 1 O LEU B1721 N LEU B1662
SHEET 7 AA4 7 THR B1748 VAL B1752 1 O THR B1748 N HIS B1722
SHEET 1 AA5 2 VAL C1540 PHE C1541 0
SHEET 2 AA5 2 LEU C1607 PRO C1608 1 O LEU C1607 N PHE C1541
SHEET 1 AA6 7 VAL C1554 GLY C1557 0
SHEET 2 AA6 7 VAL C1593 LEU C1596 -1 O VAL C1593 N LEU C1556
SHEET 3 AA6 7 THR C1564 CYS C1568 1 N CYS C1567 O THR C1594
SHEET 4 AA6 7 PHE C1631 HIS C1636 1 O VAL C1632 N VAL C1566
SHEET 5 AA6 7 ALA C1659 MET C1663 1 O VAL C1661 N LEU C1633
SHEET 6 AA6 7 VAL C1720 GLU C1727 1 O LEU C1721 N LEU C1660
SHEET 7 AA6 7 THR C1748 THR C1755 1 O THR C1748 N HIS C1722
SHEET 1 AA7 2 VAL D1540 PHE D1541 0
SHEET 2 AA7 2 LEU D1607 PRO D1608 1 O LEU D1607 N PHE D1541
SHEET 1 AA8 7 VAL D1554 GLY D1557 0
SHEET 2 AA8 7 VAL D1593 LEU D1596 -1 O VAL D1593 N LEU D1556
SHEET 3 AA8 7 THR D1564 CYS D1568 1 N CYS D1567 O THR D1594
SHEET 4 AA8 7 PHE D1631 HIS D1636 1 O VAL D1632 N VAL D1566
SHEET 5 AA8 7 ALA D1659 MET D1663 1 O MET D1663 N GLY D1635
SHEET 6 AA8 7 VAL D1720 ALA D1725 1 O LEU D1721 N LEU D1662
SHEET 7 AA8 7 THR D1748 VAL D1752 1 O VAL D1752 N TYR D1724
CRYST1 63.340 95.666 83.118 90.00 93.67 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 0.015788 0.000000 0.001013 0.00000
SCALE2 0.000000 0.010453 0.000000 0.00000
SCALE3 0.000000 0.000000 0.012056 0.00000
TER 1794 VAL A1778
TER 3630 VAL B1778
TER 5522 VAL C1778
TER 7452 VAL D1778
MASTER 333 0 0 42 36 0 0 6 7700 4 0 84
END |