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HEADER HYDROLASE 22-DEC-19 6TT0
TITLE CRYSTAL STRUCTURE OF A POTENT AND REVERSIBLE DUAL BINDING SITE
TITLE 2 ACETYLCHOLINESTERASE CHIRAL INHIBITOR
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ACETYLCHOLINESTERASE;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: ACHE;
COMPND 5 EC: 3.1.1.7;
COMPND 6 ENGINEERED: YES;
COMPND 7 OTHER_DETAILS: T. CALIFORNICA ACETYLCHOLINESTERASE
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: TETRONARCE CALIFORNICA;
SOURCE 3 ORGANISM_COMMON: PACIFIC ELECTRIC RAY;
SOURCE 4 ORGANISM_TAXID: 7787;
SOURCE 5 GENE: ACHE;
SOURCE 6 EXPRESSION_SYSTEM: TETRONARCE CALIFORNICA;
SOURCE 7 EXPRESSION_SYSTEM_COMMON: PACIFIC ELECTRIC RAY;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 7787
KEYWDS DUAL BINDING SITE INHIBITOR, CHIRAL SEPARATION, ACETYLCHOLINESTERASE,
KEYWDS 2 ALZHEIMER'S DISEASE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR E.DE LA MORA,G.F.MANGIATORDI,B.D.BELVISO,R.CALIANDRO,J.P.COLLETIER,
AUTHOR 2 M.CATTO
REVDAT 1 10-JUN-20 6TT0 0
JRNL AUTH M.CATTO,L.PISANI,E.DE LA MORA,B.D.BELVISO,G.F.MANGIATORDI,
JRNL AUTH 2 A.PINTO,A.PALMA,N.DENORA,R.CALIANDRO,J.P.COLLETIER,I.SILMAN,
JRNL AUTH 3 O.NICOLOTTI,C.D.ALTOMARE
JRNL TITL CHIRAL SEPARATION, X-RAY STRUCTURE, AND BIOLOGICAL
JRNL TITL 2 EVALUATION OF A POTENT AND REVERSIBLE DUAL BINDING SITE ACHE
JRNL TITL 3 INHIBITOR.
JRNL REF ACS MED.CHEM.LETT. V. 11 869 2020
JRNL REFN ISSN 1948-5875
JRNL PMID 32435398
JRNL DOI 10.1021/ACSMEDCHEMLETT.9B00656
REMARK 2
REMARK 2 RESOLUTION. 2.80 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.11.1_2575
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) : 2.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 39.48
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.349
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.1
REMARK 3 NUMBER OF REFLECTIONS : 24321
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.191
REMARK 3 R VALUE (WORKING SET) : 0.188
REMARK 3 FREE R VALUE : 0.235
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.889
REMARK 3 FREE R VALUE TEST SET COUNT : 1189
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 39.4798 - 5.5954 0.95 2942 172 0.1771 0.2134
REMARK 3 2 5.5954 - 4.4432 0.98 2890 163 0.1534 0.2025
REMARK 3 3 4.4432 - 3.8821 0.98 2912 142 0.1631 0.2342
REMARK 3 4 3.8821 - 3.5274 0.99 2903 132 0.1737 0.2153
REMARK 3 5 3.5274 - 3.2747 0.98 2867 138 0.2164 0.2556
REMARK 3 6 3.2747 - 3.0817 0.99 2891 145 0.2407 0.3200
REMARK 3 7 3.0817 - 2.9274 0.99 2857 145 0.2814 0.3272
REMARK 3 8 2.9274 - 2.8000 0.99 2870 152 0.3208 0.3564
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) : 0.396
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 27.377
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 67.68
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 69.95
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 : 0.031 4435
REMARK 3 ANGLE : 1.363 6027
REMARK 3 CHIRALITY : 0.070 632
REMARK 3 PLANARITY : 0.007 781
REMARK 3 DIHEDRAL : 18.649 1614
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 6TT0 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 23-DEC-19.
REMARK 100 THE DEPOSITION ID IS D_1292106018.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 28-AUG-17
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID29
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.074
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 : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 24409
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.800
REMARK 200 RESOLUTION RANGE LOW (A) : 39.480
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.500
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.1
REMARK 200 DATA REDUNDANCY : 1.800
REMARK 200 R MERGE (I) : 0.04067
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 10.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.80
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.90
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.8
REMARK 200 DATA REDUNDANCY IN SHELL : 1.80
REMARK 200 R MERGE FOR SHELL (I) : 0.37680
REMARK 200 R SYM FOR SHELL (I) : 0.53280
REMARK 200 FOR SHELL : 1.570
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: 2VT7
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 70.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.10
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 32% PEG 200 100 MM MES PH 5.5, VAPOR
REMARK 280 DIFFUSION, HANGING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+1/3
REMARK 290 3555 -X+Y,-X,Z+2/3
REMARK 290 4555 Y,X,-Z
REMARK 290 5555 X-Y,-Y,-Z+2/3
REMARK 290 6555 -X,-X+Y,-Z+1/3
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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 45.79000
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 91.58000
REMARK 290 SMTRY1 4 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 4 0.866025 0.500000 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 0.00000
REMARK 290 SMTRY2 5 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 91.58000
REMARK 290 SMTRY1 6 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 45.79000
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 410 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 20650 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 6.0 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 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 GLU A 536
REMARK 465 THR A 537
REMARK 465 ILE A 538
REMARK 465 ASP A 539
REMARK 465 GLU A 540
REMARK 465 ALA A 541
REMARK 465 GLU A 542
REMARK 465 ARG A 543
REMARK 465 GLN A 544
REMARK 465 TRP A 545
REMARK 465 LYS A 546
REMARK 465 THR A 547
REMARK 465 GLU A 548
REMARK 465 PHE A 549
REMARK 465 HIS A 550
REMARK 465 ARG A 551
REMARK 465 TRP A 552
REMARK 465 SER A 553
REMARK 465 SER A 554
REMARK 465 TYR A 555
REMARK 465 MET A 556
REMARK 465 MET A 557
REMARK 465 HIS A 558
REMARK 465 TRP A 559
REMARK 465 LYS A 560
REMARK 465 ASN A 561
REMARK 465 GLN A 562
REMARK 465 PHE A 563
REMARK 465 ASP A 564
REMARK 465 HIS A 565
REMARK 465 TYR A 566
REMARK 465 SER A 567
REMARK 465 ARG A 568
REMARK 465 HIS A 569
REMARK 465 GLU A 570
REMARK 465 SER A 571
REMARK 465 CYS A 572
REMARK 465 ALA A 573
REMARK 465 GLU A 574
REMARK 465 LEU A 575
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 ND2 ASN A 416 C1 NAG A 603 1.00
REMARK 500 SG CYS A 67 CB CYS A 94 1.74
REMARK 500 CG ASN A 416 C1 NAG A 603 1.88
REMARK 500 ND2 ASN A 416 O5 NAG A 603 1.89
REMARK 500 CB CYS A 67 SG CYS A 94 1.93
REMARK 500 ND2 ASN A 416 C2 NAG A 603 2.09
REMARK 500 OE1 GLU A 5 OG SER A 103 2.10
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
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,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
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 ATM2 ATM3
REMARK 500 CYS A 94 CA - CB - SG ANGL. DEV. = 10.3 DEGREES
REMARK 500 PRO A 104 C - N - CD ANGL. DEV. = 15.4 DEGREES
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 SER A 24 12.82 59.16
REMARK 500 SER A 25 -165.58 -129.28
REMARK 500 PHE A 45 -3.84 81.07
REMARK 500 ALA A 60 52.07 -93.36
REMARK 500 LEU A 95 80.92 -64.70
REMARK 500 SER A 108 76.38 -153.77
REMARK 500 PHE A 120 -3.11 71.81
REMARK 500 PHE A 155 19.89 -143.06
REMARK 500 THR A 193 59.18 -152.20
REMARK 500 SER A 200 -128.95 51.82
REMARK 500 GLU A 299 -67.92 -106.36
REMARK 500 THR A 317 -155.73 -159.27
REMARK 500 VAL A 360 66.83 -118.44
REMARK 500 ASP A 380 59.21 -152.19
REMARK 500 ASN A 382 40.92 -100.51
REMARK 500 VAL A 400 -70.47 -136.21
REMARK 500 GLU A 455 13.98 -145.76
REMARK 500 ASN A 457 74.51 60.46
REMARK 500 HIS A 486 75.04 51.70
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 NAG A 603
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue N9T A 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue NAG A 603
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG A 602 bound
REMARK 800 to ASN A 59
DBREF 6TT0 A 4 575 UNP P04058 ACES_TETCF 25 596
SEQRES 1 A 572 SER GLU LEU LEU VAL ASN THR LYS SER GLY LYS VAL MET
SEQRES 2 A 572 GLY THR ARG VAL PRO VAL LEU SER SER HIS ILE SER ALA
SEQRES 3 A 572 PHE LEU GLY ILE PRO PHE ALA GLU PRO PRO VAL GLY ASN
SEQRES 4 A 572 MET ARG PHE ARG ARG PRO GLU PRO LYS LYS PRO TRP SER
SEQRES 5 A 572 GLY VAL TRP ASN ALA SER THR TYR PRO ASN ASN CYS GLN
SEQRES 6 A 572 GLN TYR VAL ASP GLU GLN PHE PRO GLY PHE SER GLY SER
SEQRES 7 A 572 GLU MET TRP ASN PRO ASN ARG GLU MET SER GLU ASP CYS
SEQRES 8 A 572 LEU TYR LEU ASN ILE TRP VAL PRO SER PRO ARG PRO LYS
SEQRES 9 A 572 SER THR THR VAL MET VAL TRP ILE TYR GLY GLY GLY PHE
SEQRES 10 A 572 TYR SER GLY SER SER THR LEU ASP VAL TYR ASN GLY LYS
SEQRES 11 A 572 TYR LEU ALA TYR THR GLU GLU VAL VAL LEU VAL SER LEU
SEQRES 12 A 572 SER TYR ARG VAL GLY ALA PHE GLY PHE LEU ALA LEU HIS
SEQRES 13 A 572 GLY SER GLN GLU ALA PRO GLY ASN VAL GLY LEU LEU ASP
SEQRES 14 A 572 GLN ARG MET ALA LEU GLN TRP VAL HIS ASP ASN ILE GLN
SEQRES 15 A 572 PHE PHE GLY GLY ASP PRO LYS THR VAL THR ILE PHE GLY
SEQRES 16 A 572 GLU SER ALA GLY GLY ALA SER VAL GLY MET HIS ILE LEU
SEQRES 17 A 572 SER PRO GLY SER ARG ASP LEU PHE ARG ARG ALA ILE LEU
SEQRES 18 A 572 GLN SER GLY SER PRO ASN CYS PRO TRP ALA SER VAL SER
SEQRES 19 A 572 VAL ALA GLU GLY ARG ARG ARG ALA VAL GLU LEU GLY ARG
SEQRES 20 A 572 ASN LEU ASN CYS ASN LEU ASN SER ASP GLU GLU LEU ILE
SEQRES 21 A 572 HIS CYS LEU ARG GLU LYS LYS PRO GLN GLU LEU ILE ASP
SEQRES 22 A 572 VAL GLU TRP ASN VAL LEU PRO PHE ASP SER ILE PHE ARG
SEQRES 23 A 572 PHE SER PHE VAL PRO VAL ILE ASP GLY GLU PHE PHE PRO
SEQRES 24 A 572 THR SER LEU GLU SER MET LEU ASN SER GLY ASN PHE LYS
SEQRES 25 A 572 LYS THR GLN ILE LEU LEU GLY VAL ASN LYS ASP GLU GLY
SEQRES 26 A 572 SER PHE PHE LEU LEU TYR GLY ALA PRO GLY PHE SER LYS
SEQRES 27 A 572 ASP SER GLU SER LYS ILE SER ARG GLU ASP PHE MET SER
SEQRES 28 A 572 GLY VAL LYS LEU SER VAL PRO HIS ALA ASN ASP LEU GLY
SEQRES 29 A 572 LEU ASP ALA VAL THR LEU GLN TYR THR ASP TRP MET ASP
SEQRES 30 A 572 ASP ASN ASN GLY ILE LYS ASN ARG ASP GLY LEU ASP ASP
SEQRES 31 A 572 ILE VAL GLY ASP HIS ASN VAL ILE CYS PRO LEU MET HIS
SEQRES 32 A 572 PHE VAL ASN LYS TYR THR LYS PHE GLY ASN GLY THR TYR
SEQRES 33 A 572 LEU TYR PHE PHE ASN HIS ARG ALA SER ASN LEU VAL TRP
SEQRES 34 A 572 PRO GLU TRP MET GLY VAL ILE HIS GLY TYR GLU ILE GLU
SEQRES 35 A 572 PHE VAL PHE GLY LEU PRO LEU VAL LYS GLU LEU ASN TYR
SEQRES 36 A 572 THR ALA GLU GLU GLU ALA LEU SER ARG ARG ILE MET HIS
SEQRES 37 A 572 TYR TRP ALA THR PHE ALA LYS THR GLY ASN PRO ASN GLU
SEQRES 38 A 572 PRO HIS SER GLN GLU SER LYS TRP PRO LEU PHE THR THR
SEQRES 39 A 572 LYS GLU GLN LYS PHE ILE ASP LEU ASN THR GLU PRO MET
SEQRES 40 A 572 LYS VAL HIS GLN ARG LEU ARG VAL GLN MET CYS VAL PHE
SEQRES 41 A 572 TRP ASN GLN PHE LEU PRO LYS LEU LEU ASN ALA THR GLU
SEQRES 42 A 572 THR ILE ASP GLU ALA GLU ARG GLN TRP LYS THR GLU PHE
SEQRES 43 A 572 HIS ARG TRP SER SER TYR MET MET HIS TRP LYS ASN GLN
SEQRES 44 A 572 PHE ASP HIS TYR SER ARG HIS GLU SER CYS ALA GLU LEU
HET N9T A 601 32
HET NAG A 602 14
HET NAG A 603 14
HETNAM N9T (1~{R},3~{S})-~{N}-(6,7-DIMETHOXY-2-OXIDANYLIDENE-
HETNAM 2 N9T CHROMEN-3-YL)-3-[(PHENYLMETHYL)AMINO]CYCLOHEXANE-1-
HETNAM 3 N9T CARBOXAMIDE
HETNAM NAG N-ACETYL-D-GLUCOSAMINE
FORMUL 2 N9T C25 H28 N2 O5
FORMUL 3 NAG 2(C8 H15 N O6)
FORMUL 5 HOH *88(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 TYR A 130 5 4
HELIX 4 AA4 ASN A 131 GLU A 140 1 10
HELIX 5 AA5 GLY A 151 LEU A 156 1 6
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 SER A 237 LEU A 252 1 16
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 SER A 311 1 8
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 THR A 376 1 13
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 VAL A 453 5 5
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 ALA A 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 MET A 16
SHEET 1 AA211 THR A 18 VAL A 22 0
SHEET 2 AA211 SER A 25 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 LEU A 146 -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 PHE A 197 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 TYR A 419 N LEU A 321
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
SSBOND 1 CYS A 254 CYS A 265 1555 1555 2.04
SSBOND 2 CYS A 402 CYS A 521 1555 1555 2.05
LINK ND2 ASN A 59 C1 NAG A 602 1555 1555 1.47
CISPEP 1 SER A 103 PRO A 104 0 2.75
SITE 1 AC1 10 TYR A 70 ASP A 72 TYR A 121 GLN A 185
SITE 2 AC1 10 GLU A 199 TRP A 279 PHE A 330 PHE A 331
SITE 3 AC1 10 HIS A 440 HOH A 749
SITE 1 AC2 1 ASN A 416
SITE 1 AC3 2 ASN A 59 HOH A 715
CRYST1 111.420 111.420 137.370 90.00 90.00 120.00 P 31 2 1 6
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 0.008975 0.005182 0.000000 0.00000
SCALE2 0.000000 0.010363 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007280 0.00000
TER 4245 THR A 535
MASTER 347 0 3 25 14 0 5 6 4392 1 65 44
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