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HEADER HYDROLASE 15-NOV-17 6EZG
TITLE TORPEDO CALIFORNICA ACETYLCHOLINESTERASE IN COMPLEX WITH MR33112
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ACETYLCHOLINESTERASE;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: ACHE;
COMPND 5 EC: 3.1.1.7
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: TETRONARCE CALIFORNICA;
SOURCE 3 ORGANISM_COMMON: PACIFIC ELECTRIC RAY;
SOURCE 4 ORGANISM_TAXID: 7787
KEYWDS ACETYLCHOLINESTERASE, MULTI-TARGET INHIBITOR, ALZHEIMER DESEASE,
KEYWDS 2 HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR G.SANTONI,J.LALUT,D.KARILA,C.LECOUTEY,A.DAVIS,F.NACHON,I.SILLMAN,
AUTHOR 2 J.SUSSMAN,M.WEIK,T.MAURICE,P.DALLEMAGNE,C.ROCHAIS
REVDAT 1 21-NOV-18 6EZG 0
JRNL AUTH J.LALUT,G.SANTONI,D.KARILA,C.LECOUTEY,A.DAVIS,F.NACHON,
JRNL AUTH 2 I.SILLMAN,J.SUSSMAN,M.WEIK,T.MAURICE,P.DALLEMAGNE,C.ROCHAIS
JRNL TITL NOVEL MULTITARGET-DIRECTED LIGANDS TARGETING
JRNL TITL 2 ACETYLCHOLINESTERASE AND SIGMA1 RECEPTORS AS LEAD COMPOUNDS
JRNL TITL 3 FOR TREATMENT OF ALZHEIMER'S DISEASE: SYNTHESIS, EVALUATION,
JRNL TITL 4 AND STRUCTURAL CHARACTERIZATION OF THEIR COMPLEXES WITH
JRNL TITL 5 ACETYLCHOLINESTERASE
JRNL REF EUR.J.MED.CHEM. 2018
JRNL REFN ISSN 0223-5234
JRNL DOI 10.1016/J.EJMECH.2018.10.064
REMARK 2
REMARK 2 RESOLUTION. 2.20 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.9_1692
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) : 2.20
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 45.42
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.0
REMARK 3 NUMBER OF REFLECTIONS : 73468
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) : 0.190
REMARK 3 FREE R VALUE : 0.237
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 3671
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 45.4300 - 6.5113 0.97 2895 153 0.1857 0.2101
REMARK 3 2 6.5113 - 5.1706 0.98 2811 123 0.1574 0.2098
REMARK 3 3 5.1706 - 4.5177 0.98 2762 148 0.1360 0.1538
REMARK 3 4 4.5177 - 4.1049 0.99 2765 141 0.1321 0.1850
REMARK 3 5 4.1049 - 3.8108 0.99 2738 155 0.1448 0.1840
REMARK 3 6 3.8108 - 3.5863 0.97 2670 169 0.1671 0.2132
REMARK 3 7 3.5863 - 3.4067 0.97 2721 144 0.1741 0.2149
REMARK 3 8 3.4067 - 3.2585 0.97 2667 154 0.1972 0.2173
REMARK 3 9 3.2585 - 3.1331 0.98 2700 132 0.2025 0.2521
REMARK 3 10 3.1331 - 3.0250 0.98 2701 166 0.2148 0.2924
REMARK 3 11 3.0250 - 2.9304 0.98 2668 144 0.2074 0.2611
REMARK 3 12 2.9304 - 2.8467 0.98 2715 152 0.2101 0.3312
REMARK 3 13 2.8467 - 2.7717 0.95 2625 116 0.2011 0.2322
REMARK 3 14 2.7717 - 2.7041 0.97 2683 116 0.2138 0.2722
REMARK 3 15 2.7041 - 2.6426 0.96 2630 148 0.2212 0.2991
REMARK 3 16 2.6426 - 2.5864 0.97 2676 146 0.2277 0.2809
REMARK 3 17 2.5864 - 2.5347 0.98 2671 150 0.2411 0.3160
REMARK 3 18 2.5347 - 2.4868 0.97 2677 134 0.2309 0.3102
REMARK 3 19 2.4868 - 2.4424 0.97 2663 134 0.2281 0.2974
REMARK 3 20 2.4424 - 2.4010 0.98 2670 125 0.2407 0.3075
REMARK 3 21 2.4010 - 2.3623 0.97 2660 139 0.2463 0.3013
REMARK 3 22 2.3623 - 2.3260 0.96 2633 127 0.2491 0.2913
REMARK 3 23 2.3260 - 2.2918 0.95 2561 143 0.2668 0.2908
REMARK 3 24 2.2918 - 2.2595 0.95 2607 134 0.2781 0.3638
REMARK 3 25 2.2595 - 2.2289 0.97 2611 149 0.2980 0.3542
REMARK 3 26 2.2289 - 2.2000 0.95 2617 129 0.3172 0.3695
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) : 0.270
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 29.470
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 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 : 0.007 8876
REMARK 3 ANGLE : 0.998 12044
REMARK 3 CHIRALITY : 0.042 1262
REMARK 3 PLANARITY : 0.005 1562
REMARK 3 DIHEDRAL : 14.316 3218
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 6EZG COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 15-NOV-17.
REMARK 100 THE DEPOSITION ID IS D_1200007514.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 26-JUN-14
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.8
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID23-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.03
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : AIMLESS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 73468
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.200
REMARK 200 RESOLUTION RANGE LOW (A) : 45.420
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.0
REMARK 200 DATA REDUNDANCY : 4.510
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 10.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.20
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.30
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: NULL
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 59.53
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.04
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 36% PEG 200 150MM MES PH 5.8, VAPOR
REMARK 280 DIFFUSION, HANGING DROP, TEMPERATURE 277K
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 45.85550
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 75.24700
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 53.49800
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 75.24700
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 45.85550
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 53.49800
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 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 3130 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 39200 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 4.0 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 ASP A 1
REMARK 465 ASP A 2
REMARK 465 HIS A 3
REMARK 465 ALA A 536
REMARK 465 CYS A 537
REMARK 465 ASP B 1
REMARK 465 ASP B 2
REMARK 465 HIS B 3
REMARK 465 ALA B 536
REMARK 465 CYS B 537
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 45 -5.92 82.05
REMARK 500 ASN A 131 108.09 -56.15
REMARK 500 SER A 200 -122.15 56.65
REMARK 500 GLU A 299 -57.91 -134.90
REMARK 500 ASN A 313 77.87 -69.28
REMARK 500 THR A 317 -167.35 -163.85
REMARK 500 ASP A 380 50.71 -163.65
REMARK 500 VAL A 400 -59.97 -121.13
REMARK 500 HIS A 486 -118.10 -68.32
REMARK 500 SER A 487 116.71 69.59
REMARK 500 ARG A 517 44.07 33.35
REMARK 500 PHE B 45 -10.05 79.68
REMARK 500 ALA B 60 48.88 -105.21
REMARK 500 SER B 108 78.99 -155.97
REMARK 500 PHE B 155 17.38 -145.67
REMARK 500 SER B 200 -120.14 58.47
REMARK 500 GLU B 299 -70.44 -121.40
REMARK 500 ASP B 380 51.30 -161.40
REMARK 500 VAL B 400 -64.04 -121.62
REMARK 500 HIS B 486 -8.15 75.37
REMARK 500 ASN B 506 -166.43 -164.77
REMARK 500 ARG B 515 74.59 52.59
REMARK 500 ARG B 517 48.27 35.14
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH A 984 DISTANCE = 7.36 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue C6K A 603
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue C6K B 603
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG B 604
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG B 605
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG A 601 bound
REMARK 800 to ASN A 59
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG A 602 bound
REMARK 800 to ASN A 416
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG B 601 bound
REMARK 800 to ASN B 59
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG B 602 bound
REMARK 800 to ASN B 416
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1EA5 RELATED DB: PDB
REMARK 900 RELATED ID: 2W75 RELATED DB: PDB
REMARK 900 RELATED ID: 1EVE RELATED DB: PDB
DBREF 6EZG A 1 537 UNP P04058 ACES_TETCF 22 558
DBREF 6EZG B 1 537 UNP P04058 ACES_TETCF 22 558
SEQRES 1 A 537 ASP ASP HIS SER GLU LEU LEU VAL ASN THR LYS SER GLY
SEQRES 2 A 537 LYS VAL MET GLY THR ARG VAL PRO VAL LEU SER SER HIS
SEQRES 3 A 537 ILE SER ALA PHE LEU GLY ILE PRO PHE ALA GLU PRO PRO
SEQRES 4 A 537 VAL GLY ASN MET ARG PHE ARG ARG PRO GLU PRO LYS LYS
SEQRES 5 A 537 PRO TRP SER GLY VAL TRP ASN ALA SER THR TYR PRO ASN
SEQRES 6 A 537 ASN CYS GLN GLN TYR VAL ASP GLU GLN PHE PRO GLY PHE
SEQRES 7 A 537 SER GLY SER GLU MET TRP ASN PRO ASN ARG GLU MET SER
SEQRES 8 A 537 GLU ASP CYS LEU TYR LEU ASN ILE TRP VAL PRO SER PRO
SEQRES 9 A 537 ARG PRO LYS SER THR THR VAL MET VAL TRP ILE TYR GLY
SEQRES 10 A 537 GLY GLY PHE TYR SER GLY SER SER THR LEU ASP VAL TYR
SEQRES 11 A 537 ASN GLY LYS TYR LEU ALA TYR THR GLU GLU VAL VAL LEU
SEQRES 12 A 537 VAL SER LEU SER TYR ARG VAL GLY ALA PHE GLY PHE LEU
SEQRES 13 A 537 ALA LEU HIS GLY SER GLN GLU ALA PRO GLY ASN VAL GLY
SEQRES 14 A 537 LEU LEU ASP GLN ARG MET ALA LEU GLN TRP VAL HIS ASP
SEQRES 15 A 537 ASN ILE GLN PHE PHE GLY GLY ASP PRO LYS THR VAL THR
SEQRES 16 A 537 ILE PHE GLY GLU SER ALA GLY GLY ALA SER VAL GLY MET
SEQRES 17 A 537 HIS ILE LEU SER PRO GLY SER ARG ASP LEU PHE ARG ARG
SEQRES 18 A 537 ALA ILE LEU GLN SER GLY SER PRO ASN CYS PRO TRP ALA
SEQRES 19 A 537 SER VAL SER VAL ALA GLU GLY ARG ARG ARG ALA VAL GLU
SEQRES 20 A 537 LEU GLY ARG ASN LEU ASN CYS ASN LEU ASN SER ASP GLU
SEQRES 21 A 537 GLU LEU ILE HIS CYS LEU ARG GLU LYS LYS PRO GLN GLU
SEQRES 22 A 537 LEU ILE ASP VAL GLU TRP ASN VAL LEU PRO PHE ASP SER
SEQRES 23 A 537 ILE PHE ARG PHE SER PHE VAL PRO VAL ILE ASP GLY GLU
SEQRES 24 A 537 PHE PHE PRO THR SER LEU GLU SER MET LEU ASN SER GLY
SEQRES 25 A 537 ASN PHE LYS LYS THR GLN ILE LEU LEU GLY VAL ASN LYS
SEQRES 26 A 537 ASP GLU GLY SER PHE PHE LEU LEU TYR GLY ALA PRO GLY
SEQRES 27 A 537 PHE SER LYS ASP SER GLU SER LYS ILE SER ARG GLU ASP
SEQRES 28 A 537 PHE MET SER GLY VAL LYS LEU SER VAL PRO HIS ALA ASN
SEQRES 29 A 537 ASP LEU GLY LEU ASP ALA VAL THR LEU GLN TYR THR ASP
SEQRES 30 A 537 TRP MET ASP ASP ASN ASN GLY ILE LYS ASN ARG ASP GLY
SEQRES 31 A 537 LEU ASP ASP ILE VAL GLY ASP HIS ASN VAL ILE CYS PRO
SEQRES 32 A 537 LEU MET HIS PHE VAL ASN LYS TYR THR LYS PHE GLY ASN
SEQRES 33 A 537 GLY THR TYR LEU TYR PHE PHE ASN HIS ARG ALA SER ASN
SEQRES 34 A 537 LEU VAL TRP PRO GLU TRP MET GLY VAL ILE HIS GLY TYR
SEQRES 35 A 537 GLU ILE GLU PHE VAL PHE GLY LEU PRO LEU VAL LYS GLU
SEQRES 36 A 537 LEU ASN TYR THR ALA GLU GLU GLU ALA LEU SER ARG ARG
SEQRES 37 A 537 ILE MET HIS TYR TRP ALA THR PHE ALA LYS THR GLY ASN
SEQRES 38 A 537 PRO ASN GLU PRO HIS SER GLN GLU SER LYS TRP PRO LEU
SEQRES 39 A 537 PHE THR THR LYS GLU GLN LYS PHE ILE ASP LEU ASN THR
SEQRES 40 A 537 GLU PRO MET LYS VAL HIS GLN ARG LEU ARG VAL GLN MET
SEQRES 41 A 537 CYS VAL PHE TRP ASN GLN PHE LEU PRO LYS LEU LEU ASN
SEQRES 42 A 537 ALA THR ALA CYS
SEQRES 1 B 537 ASP ASP HIS SER GLU LEU LEU VAL ASN THR LYS SER GLY
SEQRES 2 B 537 LYS VAL MET GLY THR ARG VAL PRO VAL LEU SER SER HIS
SEQRES 3 B 537 ILE SER ALA PHE LEU GLY ILE PRO PHE ALA GLU PRO PRO
SEQRES 4 B 537 VAL GLY ASN MET ARG PHE ARG ARG PRO GLU PRO LYS LYS
SEQRES 5 B 537 PRO TRP SER GLY VAL TRP ASN ALA SER THR TYR PRO ASN
SEQRES 6 B 537 ASN CYS GLN GLN TYR VAL ASP GLU GLN PHE PRO GLY PHE
SEQRES 7 B 537 SER GLY SER GLU MET TRP ASN PRO ASN ARG GLU MET SER
SEQRES 8 B 537 GLU ASP CYS LEU TYR LEU ASN ILE TRP VAL PRO SER PRO
SEQRES 9 B 537 ARG PRO LYS SER THR THR VAL MET VAL TRP ILE TYR GLY
SEQRES 10 B 537 GLY GLY PHE TYR SER GLY SER SER THR LEU ASP VAL TYR
SEQRES 11 B 537 ASN GLY LYS TYR LEU ALA TYR THR GLU GLU VAL VAL LEU
SEQRES 12 B 537 VAL SER LEU SER TYR ARG VAL GLY ALA PHE GLY PHE LEU
SEQRES 13 B 537 ALA LEU HIS GLY SER GLN GLU ALA PRO GLY ASN VAL GLY
SEQRES 14 B 537 LEU LEU ASP GLN ARG MET ALA LEU GLN TRP VAL HIS ASP
SEQRES 15 B 537 ASN ILE GLN PHE PHE GLY GLY ASP PRO LYS THR VAL THR
SEQRES 16 B 537 ILE PHE GLY GLU SER ALA GLY GLY ALA SER VAL GLY MET
SEQRES 17 B 537 HIS ILE LEU SER PRO GLY SER ARG ASP LEU PHE ARG ARG
SEQRES 18 B 537 ALA ILE LEU GLN SER GLY SER PRO ASN CYS PRO TRP ALA
SEQRES 19 B 537 SER VAL SER VAL ALA GLU GLY ARG ARG ARG ALA VAL GLU
SEQRES 20 B 537 LEU GLY ARG ASN LEU ASN CYS ASN LEU ASN SER ASP GLU
SEQRES 21 B 537 GLU LEU ILE HIS CYS LEU ARG GLU LYS LYS PRO GLN GLU
SEQRES 22 B 537 LEU ILE ASP VAL GLU TRP ASN VAL LEU PRO PHE ASP SER
SEQRES 23 B 537 ILE PHE ARG PHE SER PHE VAL PRO VAL ILE ASP GLY GLU
SEQRES 24 B 537 PHE PHE PRO THR SER LEU GLU SER MET LEU ASN SER GLY
SEQRES 25 B 537 ASN PHE LYS LYS THR GLN ILE LEU LEU GLY VAL ASN LYS
SEQRES 26 B 537 ASP GLU GLY SER PHE PHE LEU LEU TYR GLY ALA PRO GLY
SEQRES 27 B 537 PHE SER LYS ASP SER GLU SER LYS ILE SER ARG GLU ASP
SEQRES 28 B 537 PHE MET SER GLY VAL LYS LEU SER VAL PRO HIS ALA ASN
SEQRES 29 B 537 ASP LEU GLY LEU ASP ALA VAL THR LEU GLN TYR THR ASP
SEQRES 30 B 537 TRP MET ASP ASP ASN ASN GLY ILE LYS ASN ARG ASP GLY
SEQRES 31 B 537 LEU ASP ASP ILE VAL GLY ASP HIS ASN VAL ILE CYS PRO
SEQRES 32 B 537 LEU MET HIS PHE VAL ASN LYS TYR THR LYS PHE GLY ASN
SEQRES 33 B 537 GLY THR TYR LEU TYR PHE PHE ASN HIS ARG ALA SER ASN
SEQRES 34 B 537 LEU VAL TRP PRO GLU TRP MET GLY VAL ILE HIS GLY TYR
SEQRES 35 B 537 GLU ILE GLU PHE VAL PHE GLY LEU PRO LEU VAL LYS GLU
SEQRES 36 B 537 LEU ASN TYR THR ALA GLU GLU GLU ALA LEU SER ARG ARG
SEQRES 37 B 537 ILE MET HIS TYR TRP ALA THR PHE ALA LYS THR GLY ASN
SEQRES 38 B 537 PRO ASN GLU PRO HIS SER GLN GLU SER LYS TRP PRO LEU
SEQRES 39 B 537 PHE THR THR LYS GLU GLN LYS PHE ILE ASP LEU ASN THR
SEQRES 40 B 537 GLU PRO MET LYS VAL HIS GLN ARG LEU ARG VAL GLN MET
SEQRES 41 B 537 CYS VAL PHE TRP ASN GLN PHE LEU PRO LYS LEU LEU ASN
SEQRES 42 B 537 ALA THR ALA CYS
HET NAG A 601 14
HET NAG A 602 14
HET C6K A 603 29
HET NAG B 601 14
HET NAG B 602 14
HET C6K B 603 29
HET PEG B 604 17
HET PEG B 605 17
HETNAM NAG N-ACETYL-D-GLUCOSAMINE
HETNAM C6K 1-(7-CHLORANYL-4-METHOXY-1~{H}-INDOL-5-YL)-3-[1-
HETNAM 2 C6K (PHENYLMETHYL)PIPERIDIN-4-YL]PROPAN-1-ONE
HETNAM PEG DI(HYDROXYETHYL)ETHER
FORMUL 3 NAG 4(C8 H15 N O6)
FORMUL 5 C6K 2(C24 H27 CL N2 O2)
FORMUL 9 PEG 2(C4 H10 O3)
FORMUL 11 HOH *564(H2 O)
HELIX 1 AA1 VAL A 40 ARG A 44 5 5
HELIX 2 AA2 PHE A 78 MET A 83 1 6
HELIX 3 AA3 LEU A 127 ASN A 131 5 5
HELIX 4 AA4 GLY A 132 GLU A 140 1 9
HELIX 5 AA5 VAL A 150 LEU A 156 1 7
HELIX 6 AA6 ASN A 167 ILE A 184 1 18
HELIX 7 AA7 GLN A 185 PHE A 187 5 3
HELIX 8 AA8 SER A 200 SER A 212 1 13
HELIX 9 AA9 SER A 212 ASP A 217 1 6
HELIX 10 AB1 VAL A 238 LEU A 252 1 15
HELIX 11 AB2 SER A 258 LYS A 269 1 12
HELIX 12 AB3 LYS A 270 GLU A 278 1 9
HELIX 13 AB4 TRP A 279 LEU A 282 5 4
HELIX 14 AB5 SER A 304 GLY A 312 1 9
HELIX 15 AB6 GLY A 328 ALA A 336 1 9
HELIX 16 AB7 SER A 348 VAL A 360 1 13
HELIX 17 AB8 ASN A 364 TYR A 375 1 12
HELIX 18 AB9 ASN A 383 VAL A 400 1 18
HELIX 19 AC1 VAL A 400 LYS A 413 1 14
HELIX 20 AC2 PRO A 433 GLY A 437 5 5
HELIX 21 AC3 GLU A 443 PHE A 448 1 6
HELIX 22 AC4 GLY A 449 ASN A 457 5 9
HELIX 23 AC5 THR A 459 GLY A 480 1 22
HELIX 24 AC6 ARG A 517 GLN A 526 1 10
HELIX 25 AC7 GLN A 526 THR A 535 1 10
HELIX 26 AC8 VAL B 40 ARG B 44 5 5
HELIX 27 AC9 PHE B 78 MET B 83 1 6
HELIX 28 AD1 LEU B 127 ASN B 131 5 5
HELIX 29 AD2 GLY B 132 GLU B 140 1 9
HELIX 30 AD3 VAL B 150 LEU B 156 1 7
HELIX 31 AD4 ASN B 167 ILE B 184 1 18
HELIX 32 AD5 GLN B 185 PHE B 187 5 3
HELIX 33 AD6 SER B 200 SER B 212 1 13
HELIX 34 AD7 SER B 215 PHE B 219 5 5
HELIX 35 AD8 VAL B 238 ASN B 251 1 14
HELIX 36 AD9 SER B 258 GLU B 268 1 11
HELIX 37 AE1 LYS B 270 GLU B 278 1 9
HELIX 38 AE2 TRP B 279 LEU B 282 5 4
HELIX 39 AE3 SER B 304 GLY B 312 1 9
HELIX 40 AE4 GLY B 328 ALA B 336 1 9
HELIX 41 AE5 SER B 348 VAL B 360 1 13
HELIX 42 AE6 ASN B 364 TYR B 375 1 12
HELIX 43 AE7 ASN B 383 VAL B 400 1 18
HELIX 44 AE8 VAL B 400 LYS B 413 1 14
HELIX 45 AE9 PRO B 433 GLY B 437 5 5
HELIX 46 AF1 GLU B 443 PHE B 448 1 6
HELIX 47 AF2 GLY B 449 ASN B 457 5 9
HELIX 48 AF3 THR B 459 GLY B 480 1 22
HELIX 49 AF4 ARG B 517 GLN B 526 1 10
HELIX 50 AF5 GLN B 526 ALA B 534 1 9
SHEET 1 AA1 3 LEU A 7 THR A 10 0
SHEET 2 AA1 3 GLY A 13 MET A 16 -1 O VAL A 15 N VAL A 8
SHEET 3 AA1 3 VAL A 57 ASN A 59 1 O TRP A 58 N LYS A 14
SHEET 1 AA211 THR A 18 PRO A 21 0
SHEET 2 AA211 HIS A 26 PRO A 34 -1 O ILE A 27 N VAL A 20
SHEET 3 AA211 TYR A 96 VAL A 101 -1 O ILE A 99 N PHE A 30
SHEET 4 AA211 VAL A 142 SER A 145 -1 O LEU A 143 N TRP A 100
SHEET 5 AA211 THR A 109 ILE A 115 1 N TRP A 114 O VAL A 144
SHEET 6 AA211 GLY A 189 GLU A 199 1 O THR A 195 N VAL A 113
SHEET 7 AA211 ARG A 221 GLN A 225 1 O GLN A 225 N GLY A 198
SHEET 8 AA211 ILE A 319 ASN A 324 1 O LEU A 320 N ALA A 222
SHEET 9 AA211 THR A 418 PHE A 423 1 O PHE A 423 N VAL A 323
SHEET 10 AA211 LYS A 501 LEU A 505 1 O LEU A 505 N PHE A 422
SHEET 11 AA211 VAL A 512 GLN A 514 -1 O HIS A 513 N PHE A 502
SHEET 1 AA3 2 VAL A 236 SER A 237 0
SHEET 2 AA3 2 VAL A 295 ILE A 296 1 O ILE A 296 N VAL A 236
SHEET 1 AA4 3 LEU B 7 ASN B 9 0
SHEET 2 AA4 3 LYS B 14 MET B 16 -1 O VAL B 15 N VAL B 8
SHEET 3 AA4 3 VAL B 57 ASN B 59 1 O TRP B 58 N MET B 16
SHEET 1 AA511 THR B 18 VAL B 22 0
SHEET 2 AA511 SER B 25 PRO B 34 -1 O SER B 25 N VAL B 22
SHEET 3 AA511 TYR B 96 VAL B 101 -1 O ILE B 99 N PHE B 30
SHEET 4 AA511 VAL B 142 SER B 145 -1 O SER B 145 N ASN B 98
SHEET 5 AA511 THR B 109 ILE B 115 1 N TRP B 114 O VAL B 144
SHEET 6 AA511 GLY B 189 GLU B 199 1 O THR B 195 N VAL B 111
SHEET 7 AA511 ARG B 221 GLN B 225 1 O GLN B 225 N GLY B 198
SHEET 8 AA511 ILE B 319 ASN B 324 1 O LEU B 320 N ALA B 222
SHEET 9 AA511 THR B 418 PHE B 423 1 O PHE B 423 N VAL B 323
SHEET 10 AA511 LYS B 501 LEU B 505 1 O ILE B 503 N PHE B 422
SHEET 11 AA511 VAL B 512 GLN B 514 -1 O HIS B 513 N PHE B 502
SHEET 1 AA6 2 VAL B 236 SER B 237 0
SHEET 2 AA6 2 VAL B 295 ILE B 296 1 O ILE B 296 N VAL B 236
SSBOND 1 CYS A 67 CYS A 94 1555 1555 2.06
SSBOND 2 CYS A 254 CYS A 265 1555 1555 2.05
SSBOND 3 CYS A 402 CYS A 521 1555 1555 2.05
SSBOND 4 CYS B 67 CYS B 94 1555 1555 2.06
SSBOND 5 CYS B 254 CYS B 265 1555 1555 2.04
SSBOND 6 CYS B 402 CYS B 521 1555 1555 2.03
LINK ND2 ASN A 59 C1 NAG A 601 1555 1555 1.45
LINK ND2 ASN A 416 C1 NAG A 602 1555 1555 1.45
LINK ND2 ASN B 59 C1 NAG B 601 1555 1555 1.46
LINK ND2 ASN B 416 C1 NAG B 602 1555 1555 1.41
CISPEP 1 SER A 103 PRO A 104 0 2.07
CISPEP 2 SER B 103 PRO B 104 0 6.90
SITE 1 AC1 10 TYR A 70 TRP A 84 GLY A 118 GLU A 199
SITE 2 AC1 10 ILE A 287 PHE A 288 PHE A 290 PHE A 330
SITE 3 AC1 10 PHE A 331 HOH A 716
SITE 1 AC2 6 TYR B 70 GLU B 199 SER B 286 PHE B 330
SITE 2 AC2 6 PHE B 331 HIS B 440
SITE 1 AC3 3 ASN B 409 GLN B 500 ASN B 525
SITE 1 AC4 2 SER B 55 VAL B 57
SITE 1 AC5 2 ASN A 59 SER A 61
SITE 1 AC6 4 ASN A 416 LEU A 494 HOH A 853 HOH A 908
SITE 1 AC7 6 ASN B 59 SER B 61 HOH B 703 HOH B 706
SITE 2 AC7 6 HOH B 826 HOH B 832
SITE 1 AC8 1 ASN B 416
CRYST1 91.711 106.996 150.494 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 0.010904 0.000000 0.000000 0.00000
SCALE2 0.000000 0.009346 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006645 0.00000
TER 4245 THR A 535
TER 8490 THR B 535
MASTER 329 0 8 50 32 0 12 6 9180 2 164 84
END |