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HEADER HYDROLASE 20-JUN-12 4FNM
TITLE THE ALPHA-ESTERASE-7 CARBOXYLESTERASE, E3, FROM THE BLOWFLY LUCILIA
TITLE 2 CUPRINA
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: E3 ALPHA-ESTERASE-7 CARBOXYLESTERASE;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES;
COMPND 5 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: LUCILIA CUPRINA;
SOURCE 3 ORGANISM_COMMON: AUSTRALIAN SHEEP BLOWFLY,GREENBOTTLE FLY;
SOURCE 4 ORGANISM_TAXID: 7375;
SOURCE 5 STRAIN: LS2;
SOURCE 6 GENE: LCAE7;
SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 9 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 11 EXPRESSION_SYSTEM_PLASMID: PETMCSIII
KEYWDS ALPHA/BETA HYDROLASE FOLD, CARBOXYLESTERASE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR C.J.JACKSON,J.-W.LIU,P.D.CARR,F.YOUNIS,G.PANDEY,C.COPPIN,T.MEIRELLES,
AUTHOR 2 D.L.OLLIS,D.S.TAWFIK,M.WEIK,J.G.OAKESHOTT
REVDAT 1 04-DEC-13 4FNM 0
JRNL AUTH C.J.JACKSON,J.W.LIU,P.D.CARR,F.YOUNUS,C.COPPIN,T.MEIRELLES,
JRNL AUTH 2 M.LETHIER,G.PANDEY,D.L.OLLIS,R.J.RUSSELL,M.WEIK,
JRNL AUTH 3 J.G.OAKESHOTT
JRNL TITL STRUCTURE AND FUNCTION OF AN INSECT ALPHA-CARBOXYLESTERASE
JRNL TITL 2 (ALPHA ESTERASE7) ASSOCIATED WITH INSECTICIDE RESISTANCE.
JRNL REF PROC.NATL.ACAD.SCI.USA V. 110 10177 2013
JRNL REFN ISSN 0027-8424
JRNL PMID 23733941
JRNL DOI 10.1073/PNAS.1304097110
REMARK 2
REMARK 2 RESOLUTION. 1.80 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.7.1_743)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VICENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-
REMARK 3 : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO,
REMARK 3 : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL
REMARK 3 : MORIARTY,REETAL PAI,RANDY READ,JANE
REMARK 3 : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM
REMARK 3 : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH,
REMARK 3 : LAURENT STORONI,TOM TERWILLIGER,PETER
REMARK 3 : ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 42.47
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.990
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.2
REMARK 3 NUMBER OF REFLECTIONS : 54447
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.171
REMARK 3 R VALUE (WORKING SET) : 0.170
REMARK 3 FREE R VALUE : 0.204
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.030
REMARK 3 FREE R VALUE TEST SET COUNT : 2737
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 42.4772 - 4.8954 0.99 2773 139 0.1620 0.1986
REMARK 3 2 4.8954 - 3.8865 1.00 2668 137 0.1447 0.1613
REMARK 3 3 3.8865 - 3.3954 1.00 2621 130 0.1470 0.1796
REMARK 3 4 3.3954 - 3.0851 1.00 2661 132 0.1605 0.1914
REMARK 3 5 3.0851 - 2.8640 1.00 2562 139 0.1709 0.2080
REMARK 3 6 2.8640 - 2.6952 1.00 2619 145 0.1703 0.1882
REMARK 3 7 2.6952 - 2.5602 1.00 2572 158 0.1774 0.2238
REMARK 3 8 2.5602 - 2.4488 1.00 2595 143 0.1792 0.2434
REMARK 3 9 2.4488 - 2.3545 0.99 2543 160 0.1762 0.2242
REMARK 3 10 2.3545 - 2.2733 0.99 2580 136 0.1728 0.1870
REMARK 3 11 2.2733 - 2.2022 0.99 2547 108 0.1756 0.2144
REMARK 3 12 2.2022 - 2.1393 0.99 2604 142 0.1688 0.2066
REMARK 3 13 2.1393 - 2.0829 0.99 2567 140 0.1754 0.2254
REMARK 3 14 2.0829 - 2.0321 0.99 2550 129 0.1873 0.2182
REMARK 3 15 2.0321 - 1.9859 0.99 2583 119 0.1935 0.2720
REMARK 3 16 1.9859 - 1.9437 0.99 2559 131 0.1951 0.2306
REMARK 3 17 1.9437 - 1.9048 0.99 2533 148 0.2053 0.2235
REMARK 3 18 1.9048 - 1.8688 0.99 2542 143 0.2106 0.2647
REMARK 3 19 1.8688 - 1.8355 0.99 2530 138 0.2033 0.2385
REMARK 3 20 1.8355 - 1.8043 0.97 2501 120 0.2154 0.2186
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : 0.35
REMARK 3 B_SOL : 34.06
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.430
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 18.730
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 28.11
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 1.24030
REMARK 3 B22 (A**2) : 1.77700
REMARK 3 B33 (A**2) : -3.01730
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -0.00000
REMARK 3 B23 (A**2) : 0.00000
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 : 0.006 4674
REMARK 3 ANGLE : 1.037 6335
REMARK 3 CHIRALITY : 0.074 679
REMARK 3 PLANARITY : 0.005 818
REMARK 3 DIHEDRAL : 14.752 1737
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 4FNM COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 21-JUN-12.
REMARK 100 THE RCSB ID CODE IS RCSB073124.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 12-MAY-10
REMARK 200 TEMPERATURE (KELVIN) : NULL
REMARK 200 PH : 4.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID14-4
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.8266
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : CHANNEL CUT SI(111) MONOCHROMATOR
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 54477
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.800
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.1
REMARK 200 DATA REDUNDANCY : 7.300
REMARK 200 R MERGE (I) : 0.10900
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 15.5500
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
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: PHASER
REMARK 200 STARTING MODEL: PDB ENTRY 4FG5 (replaced by 5IKX)
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 45.43
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.25
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 100MM PEGMME 2K PH 4.5, VAPOR
REMARK 280 DIFFUSION, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -X,Y,-Z+1/2
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z
REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 8555 X+1/2,-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 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 113.20000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 113.20000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 25.32500
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 51.37000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 25.32500
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 51.37000
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 113.20000
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 25.32500
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 51.37000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 113.20000
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 25.32500
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 51.37000
REMARK 290 SMTRY3 8 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: 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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2750 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 41930 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 1.0 KCAL/MOL
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 350 BIOMT1 2 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 LYS A 14 CG CD CE NZ
REMARK 470 ASP A 83 CG OD1 OD2
REMARK 470 GLU A 124 CG CD OE1 OE2
REMARK 470 GLN A 319 CG CD OE1 NE2
REMARK 470 LYS A 360 CG CD CE NZ
REMARK 470 GLN A 361 CG CD OE1 NE2
REMARK 470 LYS A 467 CG CD CE NZ
REMARK 470 LYS A 489 CG CD CE NZ
REMARK 470 LYS A 495 CG CD CE NZ
REMARK 470 ASN A 523 CG OD1 ND2
REMARK 470 LYS A 531 CG CD CE NZ
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 O HOH A 1112 O HOH A 1112 4555 2.16
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 73 -2.50 72.22
REMARK 500 ASN A 120 109.42 -163.30
REMARK 500 SER A 218 -119.38 60.68
REMARK 500 TYR A 350 59.41 -148.23
REMARK 500 PHE A 421 -63.11 -131.24
REMARK 500 HIS A 435 46.67 -149.77
REMARK 500 HIS A 471 129.52 -38.66
REMARK 500 THR A 472 -11.54 86.81
REMARK 500 MET A 521 32.88 -95.09
REMARK 500 SER A 542 -141.50 -126.35
REMARK 500 HIS A 566 52.30 -143.43
REMARK 500
REMARK 500 REMARK: NULL
REMARK 610
REMARK 610 MISSING HETEROATOM
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 610 I=INSERTION CODE):
REMARK 610 M RES C SSEQI
REMARK 610 DPF A 601
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DPF A 601
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4FG5(5IKX) RELATED DB: PDB
REMARK 900 APO ENZYME IN P2(1)
REMARK 900 RELATED ID: 4FNG RELATED DB: PDB
REMARK 900 APO ENZYME IN C222(1)
DBREF 4FNM A 2 570 UNP Q25252 Q25252_LUCCU 2 570
SEQADV 4FNM LEU A 364 UNP Q25252 MET 364 ENGINEERED MUTATION
SEQADV 4FNM PHE A 419 UNP Q25252 ILE 419 ENGINEERED MUTATION
SEQADV 4FNM THR A 472 UNP Q25252 ALA 472 ENGINEERED MUTATION
SEQADV 4FNM THR A 505 UNP Q25252 ILE 505 ENGINEERED MUTATION
SEQADV 4FNM GLU A 530 UNP Q25252 LYS 530 ENGINEERED MUTATION
SEQADV 4FNM GLY A 554 UNP Q25252 ASP 554 ENGINEERED MUTATION
SEQRES 1 A 569 ASN PHE ASN VAL SER LEU MET GLU LYS LEU LYS TRP LYS
SEQRES 2 A 569 ILE LYS CYS ILE GLU ASN LYS PHE LEU ASN TYR ARG LEU
SEQRES 3 A 569 THR THR ASN GLU THR VAL VAL ALA GLU THR GLU TYR GLY
SEQRES 4 A 569 LYS VAL LYS GLY VAL LYS ARG LEU THR VAL TYR ASP ASP
SEQRES 5 A 569 SER TYR TYR SER PHE GLU GLY ILE PRO TYR ALA GLN PRO
SEQRES 6 A 569 PRO VAL GLY GLU LEU ARG PHE LYS ALA PRO GLN ARG PRO
SEQRES 7 A 569 THR PRO TRP ASP GLY VAL ARG ASP CYS CYS ASN HIS LYS
SEQRES 8 A 569 ASP LYS SER VAL GLN VAL ASP PHE ILE THR GLY LYS VAL
SEQRES 9 A 569 CYS GLY SER GLU ASP CYS LEU TYR LEU SER VAL TYR THR
SEQRES 10 A 569 ASN ASN LEU ASN PRO GLU THR LYS ARG PRO VAL LEU VAL
SEQRES 11 A 569 TYR ILE HIS GLY GLY GLY PHE ILE ILE GLY GLU ASN HIS
SEQRES 12 A 569 ARG ASP MET TYR GLY PRO ASP TYR PHE ILE LYS LYS ASP
SEQRES 13 A 569 VAL VAL LEU ILE ASN ILE GLN TYR ARG LEU GLY ALA LEU
SEQRES 14 A 569 GLY PHE LEU SER LEU ASN SER GLU ASP LEU ASN VAL PRO
SEQRES 15 A 569 GLY ASN ALA GLY LEU LYS ASP GLN VAL MET ALA LEU ARG
SEQRES 16 A 569 TRP ILE LYS ASN ASN CYS ALA ASN PHE GLY GLY ASN PRO
SEQRES 17 A 569 ASP ASN ILE THR VAL PHE GLY GLU SER ALA GLY ALA ALA
SEQRES 18 A 569 SER THR HIS TYR MET MET LEU THR GLU GLN THR ARG GLY
SEQRES 19 A 569 LEU PHE HIS ARG GLY ILE LEU MET SER GLY ASN ALA ILE
SEQRES 20 A 569 CYS PRO TRP ALA ASN THR GLN CYS GLN HIS ARG ALA PHE
SEQRES 21 A 569 THR LEU ALA LYS LEU ALA GLY TYR LYS GLY GLU ASP ASN
SEQRES 22 A 569 ASP LYS ASP VAL LEU GLU PHE LEU MET LYS ALA LYS PRO
SEQRES 23 A 569 GLN ASP LEU ILE LYS LEU GLU GLU LYS VAL LEU THR LEU
SEQRES 24 A 569 GLU GLU ARG THR ASN LYS VAL MET PHE PRO PHE GLY PRO
SEQRES 25 A 569 THR VAL GLU PRO TYR GLN THR ALA ASP CYS VAL LEU PRO
SEQRES 26 A 569 LYS HIS PRO ARG GLU MET VAL LYS THR ALA TRP GLY ASN
SEQRES 27 A 569 SER ILE PRO THR MET MET GLY ASN THR SER TYR GLU GLY
SEQRES 28 A 569 LEU PHE PHE THR SER ILE LEU LYS GLN MET PRO LEU LEU
SEQRES 29 A 569 VAL LYS GLU LEU GLU THR CYS VAL ASN PHE VAL PRO SER
SEQRES 30 A 569 GLU LEU ALA ASP ALA GLU ARG THR ALA PRO GLU THR LEU
SEQRES 31 A 569 GLU MET GLY ALA LYS ILE LYS LYS ALA HIS VAL THR GLY
SEQRES 32 A 569 GLU THR PRO THR ALA ASP ASN PHE MET ASP LEU CYS SER
SEQRES 33 A 569 HIS PHE TYR PHE TRP PHE PRO MET HIS ARG LEU LEU GLN
SEQRES 34 A 569 LEU ARG PHE ASN HIS THR SER GLY THR PRO VAL TYR LEU
SEQRES 35 A 569 TYR ARG PHE ASP PHE ASP SER GLU ASP LEU ILE ASN PRO
SEQRES 36 A 569 TYR ARG ILE MET ARG SER GLY ARG GLY VAL LYS GLY VAL
SEQRES 37 A 569 SER HIS THR ASP GLU LEU THR TYR PHE PHE TRP ASN GLN
SEQRES 38 A 569 LEU ALA LYS ARG MET PRO LYS GLU SER ARG GLU TYR LYS
SEQRES 39 A 569 THR ILE GLU ARG MET THR GLY ILE TRP THR GLN PHE ALA
SEQRES 40 A 569 THR THR GLY ASN PRO TYR SER ASN GLU ILE GLU GLY MET
SEQRES 41 A 569 GLU ASN VAL SER TRP ASP PRO ILE GLU LYS SER ASP GLU
SEQRES 42 A 569 VAL TYR LYS CYS LEU ASN ILE SER ASP GLU LEU LYS MET
SEQRES 43 A 569 ILE ASP VAL PRO GLU MET GLY LYS ILE LYS GLN TRP GLU
SEQRES 44 A 569 SER MET PHE GLU LYS HIS ARG ASP LEU PHE
HET DPF A 601 8
HETNAM DPF DIETHYL HYDROGEN PHOSPHATE
FORMUL 2 DPF C4 H11 O4 P
FORMUL 3 HOH *533(H2 O)
HELIX 1 1 SER A 6 LEU A 27 1 22
HELIX 2 2 VAL A 68 ARG A 72 5 5
HELIX 3 3 TYR A 152 LYS A 156 5 5
HELIX 4 4 LEU A 167 LEU A 173 1 7
HELIX 5 5 SER A 177 ASN A 181 5 5
HELIX 6 6 ASN A 185 CYS A 202 1 18
HELIX 7 7 ALA A 203 PHE A 205 5 3
HELIX 8 8 SER A 218 THR A 230 1 13
HELIX 9 9 GLU A 231 ARG A 234 5 4
HELIX 10 10 CYS A 249 ASN A 253 5 5
HELIX 11 11 HIS A 258 ALA A 267 1 10
HELIX 12 12 ASN A 274 ALA A 285 1 12
HELIX 13 13 LYS A 286 GLU A 294 1 9
HELIX 14 14 GLU A 295 VAL A 297 5 3
HELIX 15 15 THR A 299 ASN A 305 1 7
HELIX 16 16 HIS A 328 LYS A 334 1 7
HELIX 17 17 THR A 335 ILE A 341 5 7
HELIX 18 18 TYR A 350 PHE A 354 5 5
HELIX 19 19 PHE A 355 MET A 362 1 8
HELIX 20 20 PRO A 363 THR A 371 5 9
HELIX 21 21 CYS A 372 VAL A 376 5 5
HELIX 22 22 ALA A 387 VAL A 402 1 16
HELIX 23 23 THR A 408 PHE A 421 1 14
HELIX 24 24 PHE A 421 ASN A 434 1 14
HELIX 25 25 ASN A 455 ARG A 461 1 7
HELIX 26 26 THR A 472 PHE A 478 5 7
HELIX 27 27 SER A 491 GLY A 511 1 21
HELIX 28 28 GLU A 552 SER A 561 1 10
HELIX 29 29 MET A 562 GLU A 564 5 3
HELIX 30 30 HIS A 566 PHE A 570 5 5
SHEET 1 A 3 THR A 28 ALA A 35 0
SHEET 2 A 3 LYS A 41 LEU A 48 -1 O GLY A 44 N VAL A 33
SHEET 3 A 3 VAL A 85 ASP A 87 1 O ARG A 86 N LYS A 43
SHEET 1 B12 THR A 28 ALA A 35 0
SHEET 2 B12 LYS A 41 LEU A 48 -1 O GLY A 44 N VAL A 33
SHEET 3 B12 SER A 54 PRO A 62 -1 O TYR A 55 N ARG A 47
SHEET 4 B12 TYR A 113 THR A 118 -1 O THR A 118 N TYR A 56
SHEET 5 B12 VAL A 159 ILE A 163 -1 O LEU A 160 N TYR A 117
SHEET 6 B12 ARG A 127 ILE A 133 1 N TYR A 132 O ILE A 161
SHEET 7 B12 GLY A 207 GLU A 217 1 O ASN A 208 N ARG A 127
SHEET 8 B12 ARG A 239 MET A 243 1 O ARG A 239 N VAL A 214
SHEET 9 B12 THR A 343 THR A 348 1 O MET A 344 N LEU A 242
SHEET 10 B12 VAL A 441 PHE A 446 1 O TYR A 442 N MET A 345
SHEET 11 B12 LYS A 537 ILE A 541 1 O ILE A 541 N ARG A 445
SHEET 12 B12 LEU A 545 ASP A 549 -1 O LYS A 546 N ASN A 540
SHEET 1 C 2 GLN A 97 VAL A 98 0
SHEET 2 C 2 VAL A 105 CYS A 106 -1 O CYS A 106 N GLN A 97
LINK OG SER A 218 P1 DPF A 601 1555 1555 1.58
SITE 1 AC1 8 GLY A 136 GLY A 137 SER A 218 ALA A 219
SITE 2 AC1 8 TYR A 457 HIS A 471 THR A 472 HOH A1208
CRYST1 50.650 102.740 226.400 90.00 90.00 90.00 C 2 2 21 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 0.019743 0.000000 0.000000 0.00000
SCALE2 0.000000 0.009733 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004417 0.00000
TER 4564 PHE A 570
MASTER 319 0 1 30 17 0 2 6 5085 1 9 44
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