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HEADER PROTEIN BINDING 19-FEB-18 6FSD
TITLE MUS MUSCULUS ACETYLCHOLINESTERASE IN COMPLEX WITH 2-(4-BIPHENYLYLOXY)-
TITLE 2 N-[3-(1-PIPERIDINYL)PROPYL]-ACETAMIDE HYDROCHLORIDE (10)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ACETYLCHOLINESTERASE;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: ACHE;
COMPND 5 EC: 3.1.1.7;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 3 ORGANISM_COMMON: MOUSE;
SOURCE 4 ORGANISM_TAXID: 10090;
SOURCE 5 GENE: ACHE;
SOURCE 6 EXPRESSION_SYSTEM: HOMO SAPIENS;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 9606;
SOURCE 8 EXPRESSION_SYSTEM_CELL_LINE: HEK293F CELLS
KEYWDS INHIBITOR, HYDROLASE, ACETYLCHOLINESTERASE, PROTEIN BINDING
EXPDTA X-RAY DIFFRACTION
AUTHOR S.KNUTSSON,C.ENGDAHL,R.KUMARI,T.KINDAHL,N.FORSGREN,C.LINDGREN,
AUTHOR 2 S.KITUR,L.KAMAU,F.EKSTROM,A.LINUSSON
REVDAT 1 31-OCT-18 6FSD 0
JRNL AUTH S.KNUTSSON,C.ENGDAHL,R.KUMARI,N.FORSGREN,C.LINDGREN,
JRNL AUTH 2 T.KINDAHL,S.KITUR,L.WACHIRA,L.KAMAU,F.J.EKSTROM,A.LINUSSON
JRNL TITL NON-COVALENT INHIBITORS OF MOSQUITO ACETYLCHOLINESTERASE 1
JRNL TITL 2 WITH RESISTANCE-BREAKING POTENCY.
JRNL REF J. MED. CHEM. 2018
JRNL REFN ISSN 1520-4804
JRNL PMID 30339371
JRNL DOI 10.1021/ACS.JMEDCHEM.8B01060
REMARK 2
REMARK 2 RESOLUTION. 2.70 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (1.10.1_2155: ???)
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 : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.70
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 39.58
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 95.0
REMARK 3 NUMBER OF REFLECTIONS : 51940
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.192
REMARK 3 R VALUE (WORKING SET) : 0.191
REMARK 3 FREE R VALUE : 0.234
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 1.990
REMARK 3 FREE R VALUE TEST SET COUNT : 1035
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 39.5818 - 5.1616 0.91 7288 150 0.1686 0.1896
REMARK 3 2 5.1616 - 4.0983 0.94 7239 142 0.1519 0.1654
REMARK 3 3 4.0983 - 3.5806 0.95 7247 147 0.1780 0.2242
REMARK 3 4 3.5806 - 3.2534 0.96 7293 136 0.2061 0.2784
REMARK 3 5 3.2534 - 3.0203 0.96 7275 158 0.2434 0.3147
REMARK 3 6 3.0203 - 2.8423 0.96 7272 155 0.2500 0.3263
REMARK 3 7 2.8423 - 2.7000 0.97 7289 147 0.2755 0.3524
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
REMARK 3 SOLVENT RADIUS : 1.11
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) : 0.360
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 28.480
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 47.96
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 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 : 0.009 8672
REMARK 3 ANGLE : 1.037 11830
REMARK 3 CHIRALITY : 0.058 1264
REMARK 3 PLANARITY : 0.007 1550
REMARK 3 DIHEDRAL : 17.137 5107
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 6FSD COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 20-FEB-18.
REMARK 100 THE DEPOSITION ID IS D_1200008547.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 11-NOV-15
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.8-7.4
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : MAX II
REMARK 200 BEAMLINE : I911-3
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0
REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL MONOCHROMATOR
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 225 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 51940
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.700
REMARK 200 RESOLUTION RANGE LOW (A) : 39.580
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 95.0
REMARK 200 DATA REDUNDANCY : 5.600
REMARK 200 R MERGE (I) : 0.07983
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 18.2200
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.70
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.80
REMARK 200 COMPLETENESS FOR SHELL (%) : 97.0
REMARK 200 DATA REDUNDANCY IN SHELL : 5.60
REMARK 200 R MERGE FOR SHELL (I) : 0.55940
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 4.020
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: FOURIER SYNTHESIS
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: 1J06
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 65.67
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.58
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 750, HEPES, VAPOR DIFFUSION,
REMARK 280 HANGING DROP, TEMPERATURE 277.15K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 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 39.00650
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 113.63050
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 55.16350
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 113.63050
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 39.00650
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 55.16350
REMARK 290 SMTRY3 4 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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 3750 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 37040 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 7.0 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 PRO A 258
REMARK 465 PRO A 259
REMARK 465 GLY A 260
REMARK 465 GLY A 261
REMARK 465 ALA A 262
REMARK 465 GLY A 263
REMARK 465 GLY A 264
REMARK 465 THR A 543
REMARK 465 ALA A 544
REMARK 465 THR A 545
REMARK 465 GLY A 546
REMARK 465 ALA A 547
REMARK 465 PRO A 548
REMARK 465 GLU B 1
REMARK 465 GLY B 2
REMARK 465 ARG B 3
REMARK 465 PRO B 258
REMARK 465 PRO B 259
REMARK 465 GLY B 260
REMARK 465 GLY B 261
REMARK 465 ALA B 262
REMARK 465 GLY B 263
REMARK 465 GLY B 264
REMARK 465 ALA B 544
REMARK 465 THR B 545
REMARK 465 GLY B 546
REMARK 465 ALA B 547
REMARK 465 PRO B 548
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 496 CG CD CE NZ
REMARK 470 ARG B 493 CG CD NE CZ NH1 NH2
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
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 RES CSSEQI ATM2 DEVIATION
REMARK 500 GLU B 81 CD GLU B 81 OE1 -0.080
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 47 -5.30 72.89
REMARK 500 CYS A 96 -3.26 -154.85
REMARK 500 ALA A 167 64.36 -157.42
REMARK 500 SER A 203 -124.05 58.63
REMARK 500 SER A 240 160.37 -49.65
REMARK 500 ASP A 306 -84.16 -126.94
REMARK 500 VAL A 367 67.06 -115.86
REMARK 500 HIS A 387 55.85 -143.65
REMARK 500 PRO A 388 2.58 -66.55
REMARK 500 VAL A 407 -65.22 -131.69
REMARK 500 ARG A 493 -74.45 -87.75
REMARK 500 ASP A 494 87.23 -35.86
REMARK 500 ALA A 506 -74.04 -56.72
REMARK 500 PRO B 41 41.77 -79.99
REMARK 500 ALA B 62 60.87 -114.11
REMARK 500 GLN B 66 -169.55 -71.19
REMARK 500 CYS B 96 -6.97 -144.74
REMARK 500 LEU B 97 74.27 -64.73
REMARK 500 ARG B 107 139.07 -39.19
REMARK 500 PHE B 123 15.30 59.35
REMARK 500 ALA B 167 64.13 -168.75
REMARK 500 SER B 203 -122.69 58.81
REMARK 500 ASP B 306 -81.44 -126.48
REMARK 500 TYR B 341 34.77 -97.53
REMARK 500 ASN B 350 -147.65 -94.85
REMARK 500 VAL B 367 68.82 -116.30
REMARK 500 VAL B 407 -61.34 -125.99
REMARK 500 SER B 495 -123.84 -83.33
REMARK 500 LYS B 496 134.94 69.46
REMARK 500 PRO B 498 85.80 -57.68
REMARK 500 ALA B 542 39.16 178.94
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 E5H A 601
REMARK 610 E5H B 601
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue E5H A 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue TOE A 602
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PG0 A 603
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue E5H B 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 1PG B 602
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PG0 B 603
DBREF 6FSD A 1 543 UNP P21836 ACES_MOUSE 32 574
DBREF 6FSD B 1 543 UNP P21836 ACES_MOUSE 32 574
SEQADV 6FSD ALA A 544 UNP P21836 EXPRESSION TAG
SEQADV 6FSD THR A 545 UNP P21836 EXPRESSION TAG
SEQADV 6FSD GLY A 546 UNP P21836 EXPRESSION TAG
SEQADV 6FSD ALA A 547 UNP P21836 EXPRESSION TAG
SEQADV 6FSD PRO A 548 UNP P21836 EXPRESSION TAG
SEQADV 6FSD ALA B 544 UNP P21836 EXPRESSION TAG
SEQADV 6FSD THR B 545 UNP P21836 EXPRESSION TAG
SEQADV 6FSD GLY B 546 UNP P21836 EXPRESSION TAG
SEQADV 6FSD ALA B 547 UNP P21836 EXPRESSION TAG
SEQADV 6FSD PRO B 548 UNP P21836 EXPRESSION TAG
SEQRES 1 A 548 GLU GLY ARG GLU ASP PRO GLN LEU LEU VAL ARG VAL ARG
SEQRES 2 A 548 GLY GLY GLN LEU ARG GLY ILE ARG LEU LYS ALA PRO GLY
SEQRES 3 A 548 GLY PRO VAL SER ALA PHE LEU GLY ILE PRO PHE ALA GLU
SEQRES 4 A 548 PRO PRO VAL GLY SER ARG ARG PHE MET PRO PRO GLU PRO
SEQRES 5 A 548 LYS ARG PRO TRP SER GLY VAL LEU ASP ALA THR THR PHE
SEQRES 6 A 548 GLN ASN VAL CYS TYR GLN TYR VAL ASP THR LEU TYR PRO
SEQRES 7 A 548 GLY PHE GLU GLY THR GLU MET TRP ASN PRO ASN ARG GLU
SEQRES 8 A 548 LEU SER GLU ASP CYS LEU TYR LEU ASN VAL TRP THR PRO
SEQRES 9 A 548 TYR PRO ARG PRO ALA SER PRO THR PRO VAL LEU ILE TRP
SEQRES 10 A 548 ILE TYR GLY GLY GLY PHE TYR SER GLY ALA ALA SER LEU
SEQRES 11 A 548 ASP VAL TYR ASP GLY ARG PHE LEU ALA GLN VAL GLU GLY
SEQRES 12 A 548 ALA VAL LEU VAL SER MET ASN TYR ARG VAL GLY THR PHE
SEQRES 13 A 548 GLY PHE LEU ALA LEU PRO GLY SER ARG GLU ALA PRO GLY
SEQRES 14 A 548 ASN VAL GLY LEU LEU ASP GLN ARG LEU ALA LEU GLN TRP
SEQRES 15 A 548 VAL GLN GLU ASN ILE ALA ALA PHE GLY GLY ASP PRO MET
SEQRES 16 A 548 SER VAL THR LEU PHE GLY GLU SER ALA GLY ALA ALA SER
SEQRES 17 A 548 VAL GLY MET HIS ILE LEU SER LEU PRO SER ARG SER LEU
SEQRES 18 A 548 PHE HIS ARG ALA VAL LEU GLN SER GLY THR PRO ASN GLY
SEQRES 19 A 548 PRO TRP ALA THR VAL SER ALA GLY GLU ALA ARG ARG ARG
SEQRES 20 A 548 ALA THR LEU LEU ALA ARG LEU VAL GLY CYS PRO PRO GLY
SEQRES 21 A 548 GLY ALA GLY GLY ASN ASP THR GLU LEU ILE ALA CYS LEU
SEQRES 22 A 548 ARG THR ARG PRO ALA GLN ASP LEU VAL ASP HIS GLU TRP
SEQRES 23 A 548 HIS VAL LEU PRO GLN GLU SER ILE PHE ARG PHE SER PHE
SEQRES 24 A 548 VAL PRO VAL VAL ASP GLY ASP PHE LEU SER ASP THR PRO
SEQRES 25 A 548 GLU ALA LEU ILE ASN THR GLY ASP PHE GLN ASP LEU GLN
SEQRES 26 A 548 VAL LEU VAL GLY VAL VAL LYS ASP GLU GLY SER TYR PHE
SEQRES 27 A 548 LEU VAL TYR GLY VAL PRO GLY PHE SER LYS ASP ASN GLU
SEQRES 28 A 548 SER LEU ILE SER ARG ALA GLN PHE LEU ALA GLY VAL ARG
SEQRES 29 A 548 ILE GLY VAL PRO GLN ALA SER ASP LEU ALA ALA GLU ALA
SEQRES 30 A 548 VAL VAL LEU HIS TYR THR ASP TRP LEU HIS PRO GLU ASP
SEQRES 31 A 548 PRO THR HIS LEU ARG ASP ALA MET SER ALA VAL VAL GLY
SEQRES 32 A 548 ASP HIS ASN VAL VAL CYS PRO VAL ALA GLN LEU ALA GLY
SEQRES 33 A 548 ARG LEU ALA ALA GLN GLY ALA ARG VAL TYR ALA TYR ILE
SEQRES 34 A 548 PHE GLU HIS ARG ALA SER THR LEU THR TRP PRO LEU TRP
SEQRES 35 A 548 MET GLY VAL PRO HIS GLY TYR GLU ILE GLU PHE ILE PHE
SEQRES 36 A 548 GLY LEU PRO LEU ASP PRO SER LEU ASN TYR THR THR GLU
SEQRES 37 A 548 GLU ARG ILE PHE ALA GLN ARG LEU MET LYS TYR TRP THR
SEQRES 38 A 548 ASN PHE ALA ARG THR GLY ASP PRO ASN ASP PRO ARG ASP
SEQRES 39 A 548 SER LYS SER PRO GLN TRP PRO PRO TYR THR THR ALA ALA
SEQRES 40 A 548 GLN GLN TYR VAL SER LEU ASN LEU LYS PRO LEU GLU VAL
SEQRES 41 A 548 ARG ARG GLY LEU ARG ALA GLN THR CYS ALA PHE TRP ASN
SEQRES 42 A 548 ARG PHE LEU PRO LYS LEU LEU SER ALA THR ALA THR GLY
SEQRES 43 A 548 ALA PRO
SEQRES 1 B 548 GLU GLY ARG GLU ASP PRO GLN LEU LEU VAL ARG VAL ARG
SEQRES 2 B 548 GLY GLY GLN LEU ARG GLY ILE ARG LEU LYS ALA PRO GLY
SEQRES 3 B 548 GLY PRO VAL SER ALA PHE LEU GLY ILE PRO PHE ALA GLU
SEQRES 4 B 548 PRO PRO VAL GLY SER ARG ARG PHE MET PRO PRO GLU PRO
SEQRES 5 B 548 LYS ARG PRO TRP SER GLY VAL LEU ASP ALA THR THR PHE
SEQRES 6 B 548 GLN ASN VAL CYS TYR GLN TYR VAL ASP THR LEU TYR PRO
SEQRES 7 B 548 GLY PHE GLU GLY THR GLU MET TRP ASN PRO ASN ARG GLU
SEQRES 8 B 548 LEU SER GLU ASP CYS LEU TYR LEU ASN VAL TRP THR PRO
SEQRES 9 B 548 TYR PRO ARG PRO ALA SER PRO THR PRO VAL LEU ILE TRP
SEQRES 10 B 548 ILE TYR GLY GLY GLY PHE TYR SER GLY ALA ALA SER LEU
SEQRES 11 B 548 ASP VAL TYR ASP GLY ARG PHE LEU ALA GLN VAL GLU GLY
SEQRES 12 B 548 ALA VAL LEU VAL SER MET ASN TYR ARG VAL GLY THR PHE
SEQRES 13 B 548 GLY PHE LEU ALA LEU PRO GLY SER ARG GLU ALA PRO GLY
SEQRES 14 B 548 ASN VAL GLY LEU LEU ASP GLN ARG LEU ALA LEU GLN TRP
SEQRES 15 B 548 VAL GLN GLU ASN ILE ALA ALA PHE GLY GLY ASP PRO MET
SEQRES 16 B 548 SER VAL THR LEU PHE GLY GLU SER ALA GLY ALA ALA SER
SEQRES 17 B 548 VAL GLY MET HIS ILE LEU SER LEU PRO SER ARG SER LEU
SEQRES 18 B 548 PHE HIS ARG ALA VAL LEU GLN SER GLY THR PRO ASN GLY
SEQRES 19 B 548 PRO TRP ALA THR VAL SER ALA GLY GLU ALA ARG ARG ARG
SEQRES 20 B 548 ALA THR LEU LEU ALA ARG LEU VAL GLY CYS PRO PRO GLY
SEQRES 21 B 548 GLY ALA GLY GLY ASN ASP THR GLU LEU ILE ALA CYS LEU
SEQRES 22 B 548 ARG THR ARG PRO ALA GLN ASP LEU VAL ASP HIS GLU TRP
SEQRES 23 B 548 HIS VAL LEU PRO GLN GLU SER ILE PHE ARG PHE SER PHE
SEQRES 24 B 548 VAL PRO VAL VAL ASP GLY ASP PHE LEU SER ASP THR PRO
SEQRES 25 B 548 GLU ALA LEU ILE ASN THR GLY ASP PHE GLN ASP LEU GLN
SEQRES 26 B 548 VAL LEU VAL GLY VAL VAL LYS ASP GLU GLY SER TYR PHE
SEQRES 27 B 548 LEU VAL TYR GLY VAL PRO GLY PHE SER LYS ASP ASN GLU
SEQRES 28 B 548 SER LEU ILE SER ARG ALA GLN PHE LEU ALA GLY VAL ARG
SEQRES 29 B 548 ILE GLY VAL PRO GLN ALA SER ASP LEU ALA ALA GLU ALA
SEQRES 30 B 548 VAL VAL LEU HIS TYR THR ASP TRP LEU HIS PRO GLU ASP
SEQRES 31 B 548 PRO THR HIS LEU ARG ASP ALA MET SER ALA VAL VAL GLY
SEQRES 32 B 548 ASP HIS ASN VAL VAL CYS PRO VAL ALA GLN LEU ALA GLY
SEQRES 33 B 548 ARG LEU ALA ALA GLN GLY ALA ARG VAL TYR ALA TYR ILE
SEQRES 34 B 548 PHE GLU HIS ARG ALA SER THR LEU THR TRP PRO LEU TRP
SEQRES 35 B 548 MET GLY VAL PRO HIS GLY TYR GLU ILE GLU PHE ILE PHE
SEQRES 36 B 548 GLY LEU PRO LEU ASP PRO SER LEU ASN TYR THR THR GLU
SEQRES 37 B 548 GLU ARG ILE PHE ALA GLN ARG LEU MET LYS TYR TRP THR
SEQRES 38 B 548 ASN PHE ALA ARG THR GLY ASP PRO ASN ASP PRO ARG ASP
SEQRES 39 B 548 SER LYS SER PRO GLN TRP PRO PRO TYR THR THR ALA ALA
SEQRES 40 B 548 GLN GLN TYR VAL SER LEU ASN LEU LYS PRO LEU GLU VAL
SEQRES 41 B 548 ARG ARG GLY LEU ARG ALA GLN THR CYS ALA PHE TRP ASN
SEQRES 42 B 548 ARG PHE LEU PRO LYS LEU LEU SER ALA THR ALA THR GLY
SEQRES 43 B 548 ALA PRO
HET E5H A 601 21
HET TOE A 602 11
HET PG0 A 603 8
HET E5H B 601 21
HET 1PG B 602 17
HET PG0 B 603 8
HETNAM E5H 2-(4-PHENYLPHENOXY)-~{N}-(3-PIPERIDIN-1-YLPROPYL)
HETNAM 2 E5H ETHANAMIDE
HETNAM TOE 2-[2-(2-METHOXY-ETHOXY)-ETHOXY]-ETHOXYL
HETNAM PG0 2-(2-METHOXYETHOXY)ETHANOL
HETNAM 1PG 2-(2-{2-[2-(2-METHOXY-ETHOXY)-ETHOXY]-ETHOXY}-ETHOXY)-
HETNAM 2 1PG ETHANOL
HETSYN PG0 PEG 6000
FORMUL 3 E5H 2(C22 H28 N2 O2)
FORMUL 4 TOE C7 H16 O4
FORMUL 5 PG0 2(C5 H12 O3)
FORMUL 7 1PG C11 H24 O6
FORMUL 9 HOH *165(H2 O)
HELIX 1 AA1 VAL A 42 ARG A 46 5 5
HELIX 2 AA2 PHE A 80 MET A 85 1 6
HELIX 3 AA3 LEU A 130 ASP A 134 5 5
HELIX 4 AA4 GLY A 135 GLU A 142 1 8
HELIX 5 AA5 VAL A 153 LEU A 159 1 7
HELIX 6 AA6 ASN A 170 ILE A 187 1 18
HELIX 7 AA7 ALA A 188 PHE A 190 5 3
HELIX 8 AA8 SER A 203 SER A 215 1 13
HELIX 9 AA9 LEU A 216 ARG A 219 5 4
HELIX 10 AB1 SER A 240 VAL A 255 1 16
HELIX 11 AB2 ASP A 266 ARG A 274 1 9
HELIX 12 AB3 PRO A 277 GLU A 285 1 9
HELIX 13 AB4 TRP A 286 LEU A 289 5 4
HELIX 14 AB5 THR A 311 GLY A 319 1 9
HELIX 15 AB6 GLY A 335 VAL A 340 1 6
HELIX 16 AB7 SER A 355 VAL A 367 1 13
HELIX 17 AB8 SER A 371 THR A 383 1 13
HELIX 18 AB9 ASP A 390 VAL A 407 1 18
HELIX 19 AC1 VAL A 407 GLN A 421 1 15
HELIX 20 AC2 PRO A 440 GLY A 444 5 5
HELIX 21 AC3 GLU A 450 PHE A 455 1 6
HELIX 22 AC4 GLY A 456 ASN A 464 5 9
HELIX 23 AC5 THR A 466 GLY A 487 1 22
HELIX 24 AC6 ARG A 525 ARG A 534 1 10
HELIX 25 AC7 ARG A 534 SER A 541 1 8
HELIX 26 AC8 ASP B 5 GLN B 7 5 3
HELIX 27 AC9 VAL B 42 ARG B 46 5 5
HELIX 28 AD1 PHE B 80 MET B 85 1 6
HELIX 29 AD2 LEU B 130 ASP B 134 5 5
HELIX 30 AD3 GLY B 135 GLY B 143 1 9
HELIX 31 AD4 VAL B 153 LEU B 159 1 7
HELIX 32 AD5 ASN B 170 ILE B 187 1 18
HELIX 33 AD6 ALA B 188 PHE B 190 5 3
HELIX 34 AD7 SER B 203 LEU B 214 1 12
HELIX 35 AD8 SER B 215 LEU B 221 5 7
HELIX 36 AD9 ALA B 241 VAL B 255 1 15
HELIX 37 AE1 ASP B 266 THR B 275 1 10
HELIX 38 AE2 PRO B 277 ASP B 283 1 7
HELIX 39 AE3 HIS B 284 LEU B 289 5 6
HELIX 40 AE4 THR B 311 GLY B 319 1 9
HELIX 41 AE5 GLY B 335 VAL B 340 1 6
HELIX 42 AE6 SER B 355 VAL B 367 1 13
HELIX 43 AE7 SER B 371 THR B 383 1 13
HELIX 44 AE8 ASP B 390 VAL B 407 1 18
HELIX 45 AE9 VAL B 407 GLN B 421 1 15
HELIX 46 AF1 PRO B 440 GLY B 444 5 5
HELIX 47 AF2 GLU B 450 PHE B 455 1 6
HELIX 48 AF3 GLY B 456 ASN B 464 5 9
HELIX 49 AF4 THR B 466 GLY B 487 1 22
HELIX 50 AF5 ARG B 525 ARG B 534 1 10
HELIX 51 AF6 ARG B 534 SER B 541 1 8
SHEET 1 AA1 3 LEU A 9 VAL A 12 0
SHEET 2 AA1 3 GLY A 15 ARG A 18 -1 O GLY A 15 N VAL A 12
SHEET 3 AA1 3 VAL A 59 ASP A 61 1 O LEU A 60 N GLN A 16
SHEET 1 AA211 ILE A 20 ALA A 24 0
SHEET 2 AA211 GLY A 27 PRO A 36 -1 O ALA A 31 N ILE A 20
SHEET 3 AA211 TYR A 98 PRO A 104 -1 O VAL A 101 N PHE A 32
SHEET 4 AA211 VAL A 145 MET A 149 -1 O SER A 148 N ASN A 100
SHEET 5 AA211 THR A 112 ILE A 118 1 N LEU A 115 O VAL A 147
SHEET 6 AA211 GLY A 192 GLU A 202 1 O SER A 196 N VAL A 114
SHEET 7 AA211 ARG A 224 GLN A 228 1 O GLN A 228 N GLY A 201
SHEET 8 AA211 GLN A 325 VAL A 331 1 O LEU A 327 N LEU A 227
SHEET 9 AA211 ARG A 424 PHE A 430 1 O PHE A 430 N VAL A 330
SHEET 10 AA211 GLN A 509 LEU A 513 1 O LEU A 513 N ILE A 429
SHEET 11 AA211 GLU A 519 ARG A 522 -1 O ARG A 521 N TYR A 510
SHEET 1 AA3 2 VAL A 68 CYS A 69 0
SHEET 2 AA3 2 LEU A 92 SER A 93 1 O SER A 93 N VAL A 68
SHEET 1 AA4 3 LEU B 9 VAL B 12 0
SHEET 2 AA4 3 GLY B 15 ARG B 18 -1 O LEU B 17 N VAL B 10
SHEET 3 AA4 3 VAL B 59 ASP B 61 1 O LEU B 60 N GLN B 16
SHEET 1 AA511 ILE B 20 ALA B 24 0
SHEET 2 AA511 GLY B 27 PRO B 36 -1 O VAL B 29 N LEU B 22
SHEET 3 AA511 TYR B 98 PRO B 104 -1 O VAL B 101 N PHE B 32
SHEET 4 AA511 VAL B 145 MET B 149 -1 O SER B 148 N ASN B 100
SHEET 5 AA511 THR B 112 ILE B 118 1 N LEU B 115 O VAL B 147
SHEET 6 AA511 GLY B 192 GLU B 202 1 O ASP B 193 N THR B 112
SHEET 7 AA511 ARG B 224 GLN B 228 1 O GLN B 228 N GLY B 201
SHEET 8 AA511 GLN B 325 VAL B 331 1 O LEU B 327 N LEU B 227
SHEET 9 AA511 ARG B 424 PHE B 430 1 O PHE B 430 N VAL B 330
SHEET 10 AA511 GLN B 509 LEU B 513 1 O LEU B 513 N ILE B 429
SHEET 11 AA511 GLU B 519 ARG B 522 -1 O ARG B 521 N TYR B 510
SHEET 1 AA6 2 VAL B 68 CYS B 69 0
SHEET 2 AA6 2 LEU B 92 SER B 93 1 O SER B 93 N VAL B 68
SHEET 1 AA7 2 VAL B 239 SER B 240 0
SHEET 2 AA7 2 VAL B 302 VAL B 303 1 O VAL B 303 N VAL B 239
SSBOND 1 CYS A 69 CYS A 96 1555 1555 2.04
SSBOND 2 CYS A 257 CYS A 272 1555 1555 2.06
SSBOND 3 CYS A 409 CYS A 529 1555 1555 2.05
SSBOND 4 CYS B 69 CYS B 96 1555 1555 2.06
SSBOND 5 CYS B 257 CYS B 272 1555 1555 2.10
SSBOND 6 CYS B 409 CYS B 529 1555 1555 2.07
CISPEP 1 TYR A 105 PRO A 106 0 1.56
CISPEP 2 TYR B 105 PRO B 106 0 9.04
SITE 1 AC1 6 TYR A 72 TYR A 124 TRP A 286 PHE A 295
SITE 2 AC1 6 TYR A 337 PHE A 338
SITE 1 AC2 4 VAL A 330 TYR A 428 LEU A 524 ARG A 525
SITE 1 AC3 4 GLN A 413 ARG A 417 ALA A 420 ARG A 534
SITE 1 AC4 5 TYR B 124 TRP B 286 PHE B 295 TYR B 337
SITE 2 AC4 5 PHE B 338
SITE 1 AC5 8 LEU A 380 HIS A 381 GLN A 527 PHE A 531
SITE 2 AC5 8 HIS B 381 GLN B 527 PHE B 531 PHE B 535
SITE 1 AC6 5 LEU B 214 LEU B 216 ARG B 219 GLY B 319
SITE 2 AC6 5 ASP B 320
CRYST1 78.013 110.327 227.261 90.00 90.00 90.00 P 21 21 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 0.012818 0.000000 0.000000 0.00000
SCALE2 0.000000 0.009064 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004400 0.00000
TER 4178 ALA A 542
TER 8337 THR B 543
MASTER 340 0 6 51 34 0 10 6 8586 2 98 86
END |