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HEADER HYDROLASE/HYDROLASE INHIBITOR 01-MAY-12 4EY8
TITLE CRYSTAL STRUCTURE OF RECOMBINANT HUMAN ACETYLCHOLINESTERASE IN COMPLEX
TITLE 2 WITH FASCICULIN-2
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ACETYLCHOLINESTERASE;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: UNP RESIDUES 33-574;
COMPND 5 SYNONYM: ACHE;
COMPND 6 EC: 3.1.1.7;
COMPND 7 ENGINEERED: YES;
COMPND 8 MOL_ID: 2;
COMPND 9 MOLECULE: FASCICULIN-2;
COMPND 10 CHAIN: B;
COMPND 11 SYNONYM: FAS-2, FAS2, ACETYLCHOLINESTERASE TOXIN F-VII, FASCICULIN-
COMPND 12 II, FAS-II, TOXIN TA1
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: ACHE;
SOURCE 6 EXPRESSION_SYSTEM: HOMO SAPIENS;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 9606;
SOURCE 8 EXPRESSION_SYSTEM_TISSUE: HEK-293;
SOURCE 9 MOL_ID: 2;
SOURCE 10 ORGANISM_SCIENTIFIC: DENDROASPIS ANGUSTICEPS;
SOURCE 11 ORGANISM_COMMON: EASTERN GREEN MAMBA;
SOURCE 12 ORGANISM_TAXID: 8618;
SOURCE 13 SECRETION: VENOM
KEYWDS ACETYLCHOLINESTERASE, HYDROLASE, FASCICULIN 2, SNAKE VENOM TOXIN,
KEYWDS 2 INHIBITOR, HYDROLASE-HYDROLASE INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR J.CHEUNG,M.RUDOLPH,F.BURSHTEYN,M.CASSIDY,E.GARY,J.LOVE,J.HEIGHT,
AUTHOR 2 M.FRANKLIN
REVDAT 1 17-OCT-12 4EY8 0
JRNL AUTH J.CHEUNG,M.J.RUDOLPH,F.BURSHTEYN,M.S.CASSIDY,E.N.GARY,
JRNL AUTH 2 J.LOVE,M.C.FRANKLIN,J.J.HEIGHT
JRNL TITL STRUCTURES OF HUMAN ACETYLCHOLINESTERASE IN COMPLEX WITH
JRNL TITL 2 PHARMACOLOGICALLY IMPORTANT LIGANDS.
JRNL REF J.MED.CHEM. 2012
JRNL REFN ISSN 0022-2623
JRNL PMID 23035744
JRNL DOI 10.1021/JM300871X
REMARK 2
REMARK 2 RESOLUTION. 2.60 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.8_1069)
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) : 2.60
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 46.38
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.8
REMARK 3 NUMBER OF REFLECTIONS : 33413
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.196
REMARK 3 R VALUE (WORKING SET) : 0.194
REMARK 3 FREE R VALUE : 0.244
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.030
REMARK 3 FREE R VALUE TEST SET COUNT : 1681
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 46.3880 - 5.9391 0.98 2795 136 0.1613 0.1875
REMARK 3 2 5.9391 - 4.7155 0.99 2703 147 0.1631 0.1857
REMARK 3 3 4.7155 - 4.1199 0.98 2638 162 0.1574 0.2096
REMARK 3 4 4.1199 - 3.7434 0.97 2646 130 0.1779 0.2310
REMARK 3 5 3.7434 - 3.4752 0.98 2618 161 0.2144 0.2980
REMARK 3 6 3.4752 - 3.2703 0.99 2652 131 0.2417 0.3020
REMARK 3 7 3.2703 - 3.1066 0.99 2667 129 0.2484 0.3220
REMARK 3 8 3.1066 - 2.9714 0.99 2659 134 0.2349 0.3074
REMARK 3 9 2.9714 - 2.8570 0.99 2653 141 0.2508 0.3374
REMARK 3 10 2.8570 - 2.7584 0.99 2654 143 0.2581 0.3179
REMARK 3 11 2.7584 - 2.6722 0.98 2616 142 0.2617 0.3539
REMARK 3 12 2.6722 - 2.5958 0.90 2431 125 0.2887 0.3804
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.30
REMARK 3 SHRINKAGE RADIUS : 1.10
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.350
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 30.820
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) : 15.70660
REMARK 3 B22 (A**2) : 15.70660
REMARK 3 B33 (A**2) : -31.41320
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 : 0.008 4829
REMARK 3 ANGLE : 1.187 6590
REMARK 3 CHIRALITY : 0.079 713
REMARK 3 PLANARITY : 0.006 859
REMARK 3 DIHEDRAL : 17.080 1765
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 4EY8 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 17-MAY-12.
REMARK 100 THE RCSB ID CODE IS RCSB072218.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 01-JAN-12
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5 - 7.8
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : NSLS
REMARK 200 BEAMLINE : X4C
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.990
REMARK 200 MONOCHROMATOR : SI(111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MAR CCD 165 MM
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 33704
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.596
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.6
REMARK 200 DATA REDUNDANCY : 5.000
REMARK 200 R MERGE (I) : 0.05400
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 11.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.60
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.64
REMARK 200 COMPLETENESS FOR SHELL (%) : 88.5
REMARK 200 DATA REDUNDANCY IN SHELL : 3.60
REMARK 200 R MERGE FOR SHELL (I) : 0.29000
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: 1B41
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 70.32
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.14
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.6 TO 2.0M AMMONIUM SULPHATE, 0.1M
REMARK 280 HEPES PH 7.5 - 7.8, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE
REMARK 280 283K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: H 3 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z
REMARK 290 3555 -X+Y,-X,Z
REMARK 290 4555 Y,X,-Z
REMARK 290 5555 X-Y,-Y,-Z
REMARK 290 6555 -X,-X+Y,-Z
REMARK 290 7555 X+2/3,Y+1/3,Z+1/3
REMARK 290 8555 -Y+2/3,X-Y+1/3,Z+1/3
REMARK 290 9555 -X+Y+2/3,-X+1/3,Z+1/3
REMARK 290 10555 Y+2/3,X+1/3,-Z+1/3
REMARK 290 11555 X-Y+2/3,-Y+1/3,-Z+1/3
REMARK 290 12555 -X+2/3,-X+Y+1/3,-Z+1/3
REMARK 290 13555 X+1/3,Y+2/3,Z+2/3
REMARK 290 14555 -Y+1/3,X-Y+2/3,Z+2/3
REMARK 290 15555 -X+Y+1/3,-X+2/3,Z+2/3
REMARK 290 16555 Y+1/3,X+2/3,-Z+2/3
REMARK 290 17555 X-Y+1/3,-Y+2/3,-Z+2/3
REMARK 290 18555 -X+1/3,-X+Y+2/3,-Z+2/3
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 0.00000
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 0.00000
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 0.00000
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 0.00000
REMARK 290 SMTRY1 7 1.000000 0.000000 0.000000 75.85250
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 43.79346
REMARK 290 SMTRY3 7 0.000000 0.000000 1.000000 82.62067
REMARK 290 SMTRY1 8 -0.500000 -0.866025 0.000000 75.85250
REMARK 290 SMTRY2 8 0.866025 -0.500000 0.000000 43.79346
REMARK 290 SMTRY3 8 0.000000 0.000000 1.000000 82.62067
REMARK 290 SMTRY1 9 -0.500000 0.866025 0.000000 75.85250
REMARK 290 SMTRY2 9 -0.866025 -0.500000 0.000000 43.79346
REMARK 290 SMTRY3 9 0.000000 0.000000 1.000000 82.62067
REMARK 290 SMTRY1 10 -0.500000 0.866025 0.000000 75.85250
REMARK 290 SMTRY2 10 0.866025 0.500000 0.000000 43.79346
REMARK 290 SMTRY3 10 0.000000 0.000000 -1.000000 82.62067
REMARK 290 SMTRY1 11 1.000000 0.000000 0.000000 75.85250
REMARK 290 SMTRY2 11 0.000000 -1.000000 0.000000 43.79346
REMARK 290 SMTRY3 11 0.000000 0.000000 -1.000000 82.62067
REMARK 290 SMTRY1 12 -0.500000 -0.866025 0.000000 75.85250
REMARK 290 SMTRY2 12 -0.866025 0.500000 0.000000 43.79346
REMARK 290 SMTRY3 12 0.000000 0.000000 -1.000000 82.62067
REMARK 290 SMTRY1 13 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 13 0.000000 1.000000 0.000000 87.58692
REMARK 290 SMTRY3 13 0.000000 0.000000 1.000000 165.24133
REMARK 290 SMTRY1 14 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 14 0.866025 -0.500000 0.000000 87.58692
REMARK 290 SMTRY3 14 0.000000 0.000000 1.000000 165.24133
REMARK 290 SMTRY1 15 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 15 -0.866025 -0.500000 0.000000 87.58692
REMARK 290 SMTRY3 15 0.000000 0.000000 1.000000 165.24133
REMARK 290 SMTRY1 16 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 16 0.866025 0.500000 0.000000 87.58692
REMARK 290 SMTRY3 16 0.000000 0.000000 -1.000000 165.24133
REMARK 290 SMTRY1 17 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 17 0.000000 -1.000000 0.000000 87.58692
REMARK 290 SMTRY3 17 0.000000 0.000000 -1.000000 165.24133
REMARK 290 SMTRY1 18 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 18 -0.866025 0.500000 0.000000 87.58692
REMARK 290 SMTRY3 18 0.000000 0.000000 -1.000000 165.24133
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 300 REMARK: DIMER
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: 2180 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 22300 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -8.0 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 GLY A 2
REMARK 465 ARG A 3
REMARK 465 GLU A 4
REMARK 465 PRO A 259
REMARK 465 GLY A 260
REMARK 465 GLY A 261
REMARK 465 THR A 262
REMARK 465 GLY A 263
REMARK 465 GLY A 264
REMARK 465 PRO A 495
REMARK 465 LYS A 496
REMARK 465 ALA A 497
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 C1 FUC A 605 C6 NAG A 606 2.17
REMARK 500 O5 FUC A 605 O6 NAG A 606 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 PRO A 25 -28.36 -37.53
REMARK 500 PHE A 47 -16.67 77.40
REMARK 500 ALA A 62 44.16 -109.88
REMARK 500 PHE A 123 3.27 57.12
REMARK 500 SER A 203 -120.46 60.58
REMARK 500 PRO A 217 -9.10 -54.95
REMARK 500 PRO A 290 -71.02 -56.90
REMARK 500 ASP A 306 -85.77 -93.87
REMARK 500 VAL A 407 -61.74 -131.59
REMARK 500 ASN A 464 46.43 -97.86
REMARK 500 ASP A 488 116.11 -160.05
REMARK 500 ARG A 493 -150.56 -125.51
REMARK 500 SER A 541 1.83 -69.73
REMARK 500 HIS B 6 158.52 172.16
REMARK 500 THR B 7 -162.28 -100.38
REMARK 500 ASP B 45 -167.87 -165.12
REMARK 500 PRO B 56 -145.67 -83.41
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 602
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 603
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 604
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FUC A 605
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 606
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 607
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BMA A 608
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 609
DBREF 4EY8 A 2 543 UNP P22303 ACES_HUMAN 33 574
DBREF 4EY8 B 1 61 UNP P0C1Z0 TXFA2_DENAN 1 61
SEQRES 1 A 542 GLY ARG GLU ASP ALA GLU LEU LEU VAL THR VAL ARG GLY
SEQRES 2 A 542 GLY ARG LEU ARG GLY ILE ARG LEU LYS THR PRO GLY GLY
SEQRES 3 A 542 PRO VAL SER ALA PHE LEU GLY ILE PRO PHE ALA GLU PRO
SEQRES 4 A 542 PRO MET GLY PRO ARG ARG PHE LEU PRO PRO GLU PRO LYS
SEQRES 5 A 542 GLN PRO TRP SER GLY VAL VAL ASP ALA THR THR PHE GLN
SEQRES 6 A 542 SER VAL CYS TYR GLN TYR VAL ASP THR LEU TYR PRO GLY
SEQRES 7 A 542 PHE GLU GLY THR GLU MET TRP ASN PRO ASN ARG GLU LEU
SEQRES 8 A 542 SER GLU ASP CYS LEU TYR LEU ASN VAL TRP THR PRO TYR
SEQRES 9 A 542 PRO ARG PRO THR SER PRO THR PRO VAL LEU VAL TRP ILE
SEQRES 10 A 542 TYR GLY GLY GLY PHE TYR SER GLY ALA SER SER LEU ASP
SEQRES 11 A 542 VAL TYR ASP GLY ARG PHE LEU VAL GLN ALA GLU ARG THR
SEQRES 12 A 542 VAL LEU VAL SER MET ASN TYR ARG VAL GLY ALA PHE GLY
SEQRES 13 A 542 PHE LEU ALA LEU PRO GLY SER ARG GLU ALA PRO GLY ASN
SEQRES 14 A 542 VAL GLY LEU LEU ASP GLN ARG LEU ALA LEU GLN TRP VAL
SEQRES 15 A 542 GLN GLU ASN VAL ALA ALA PHE GLY GLY ASP PRO THR SER
SEQRES 16 A 542 VAL THR LEU PHE GLY GLU SER ALA GLY ALA ALA SER VAL
SEQRES 17 A 542 GLY MET HIS LEU LEU SER PRO PRO SER ARG GLY LEU PHE
SEQRES 18 A 542 HIS ARG ALA VAL LEU GLN SER GLY ALA PRO ASN GLY PRO
SEQRES 19 A 542 TRP ALA THR VAL GLY MET GLY GLU ALA ARG ARG ARG ALA
SEQRES 20 A 542 THR GLN LEU ALA HIS LEU VAL GLY CYS PRO PRO GLY GLY
SEQRES 21 A 542 THR GLY GLY ASN ASP THR GLU LEU VAL ALA CYS LEU ARG
SEQRES 22 A 542 THR ARG PRO ALA GLN VAL LEU VAL ASN HIS GLU TRP HIS
SEQRES 23 A 542 VAL LEU PRO GLN GLU SER VAL PHE ARG PHE SER PHE VAL
SEQRES 24 A 542 PRO VAL VAL ASP GLY ASP PHE LEU SER ASP THR PRO GLU
SEQRES 25 A 542 ALA LEU ILE ASN ALA GLY ASP PHE HIS GLY LEU GLN VAL
SEQRES 26 A 542 LEU VAL GLY VAL VAL LYS ASP GLU GLY SER TYR PHE LEU
SEQRES 27 A 542 VAL TYR GLY ALA PRO GLY PHE SER LYS ASP ASN GLU SER
SEQRES 28 A 542 LEU ILE SER ARG ALA GLU PHE LEU ALA GLY VAL ARG VAL
SEQRES 29 A 542 GLY VAL PRO GLN VAL SER ASP LEU ALA ALA GLU ALA VAL
SEQRES 30 A 542 VAL LEU HIS TYR THR ASP TRP LEU HIS PRO GLU ASP PRO
SEQRES 31 A 542 ALA ARG LEU ARG GLU ALA LEU SER ASP VAL VAL GLY ASP
SEQRES 32 A 542 HIS ASN VAL VAL CYS PRO VAL ALA GLN LEU ALA GLY ARG
SEQRES 33 A 542 LEU ALA ALA GLN GLY ALA ARG VAL TYR ALA TYR VAL PHE
SEQRES 34 A 542 GLU HIS ARG ALA SER THR LEU SER TRP PRO LEU TRP MET
SEQRES 35 A 542 GLY VAL PRO HIS GLY TYR GLU ILE GLU PHE ILE PHE GLY
SEQRES 36 A 542 ILE PRO LEU ASP PRO SER ARG ASN TYR THR ALA GLU GLU
SEQRES 37 A 542 LYS ILE PHE ALA GLN ARG LEU MET ARG TYR TRP ALA ASN
SEQRES 38 A 542 PHE ALA ARG THR GLY ASP PRO ASN GLU PRO ARG ASP PRO
SEQRES 39 A 542 LYS ALA PRO GLN TRP PRO PRO TYR THR ALA GLY ALA GLN
SEQRES 40 A 542 GLN TYR VAL SER LEU ASP LEU ARG PRO LEU GLU VAL ARG
SEQRES 41 A 542 ARG GLY LEU ARG ALA GLN ALA CYS ALA PHE TRP ASN ARG
SEQRES 42 A 542 PHE LEU PRO LYS LEU LEU SER ALA THR
SEQRES 1 B 61 THR MET CYS TYR SER HIS THR THR THR SER ARG ALA ILE
SEQRES 2 B 61 LEU THR ASN CYS GLY GLU ASN SER CYS TYR ARG LYS SER
SEQRES 3 B 61 ARG ARG HIS PRO PRO LYS MET VAL LEU GLY ARG GLY CYS
SEQRES 4 B 61 GLY CYS PRO PRO GLY ASP ASP ASN LEU GLU VAL LYS CYS
SEQRES 5 B 61 CYS THR SER PRO ASP LYS CYS ASN TYR
MODRES 4EY8 ASN A 464 ASN GLYCOSYLATION SITE
MODRES 4EY8 ASN A 350 ASN GLYCOSYLATION SITE
HET SO4 A 601 5
HET SO4 A 602 5
HET SO4 A 603 5
HET SO4 A 604 5
HET FUC A 605 10
HET NAG A 606 14
HET NAG A 607 14
HET BMA A 608 11
HET NAG A 609 14
HETNAM SO4 SULFATE ION
HETNAM FUC ALPHA-L-FUCOSE
HETNAM NAG N-ACETYL-D-GLUCOSAMINE
HETNAM BMA BETA-D-MANNOSE
FORMUL 3 SO4 4(O4 S 2-)
FORMUL 7 FUC C6 H12 O5
FORMUL 7 NAG 3(C8 H15 N O6)
FORMUL 7 BMA C6 H12 O6
FORMUL 9 HOH *44(H2 O)
HELIX 1 1 MET A 42 ARG A 46 5 5
HELIX 2 2 PHE A 80 MET A 85 1 6
HELIX 3 3 LEU A 130 ASP A 134 5 5
HELIX 4 4 GLY A 135 ARG A 143 1 9
HELIX 5 5 VAL A 153 LEU A 159 1 7
HELIX 6 6 ASN A 170 VAL A 187 1 18
HELIX 7 7 ALA A 188 PHE A 190 5 3
HELIX 8 8 SER A 203 LEU A 213 1 11
HELIX 9 9 SER A 215 PHE A 222 5 8
HELIX 10 10 GLY A 240 VAL A 255 1 16
HELIX 11 11 ASP A 266 ARG A 276 1 11
HELIX 12 12 PRO A 277 TRP A 286 1 10
HELIX 13 13 HIS A 287 LEU A 289 5 3
HELIX 14 14 THR A 311 GLY A 319 1 9
HELIX 15 15 GLY A 335 GLY A 342 5 8
HELIX 16 16 SER A 355 VAL A 367 1 13
HELIX 17 17 SER A 371 THR A 383 1 13
HELIX 18 18 ASP A 390 VAL A 407 1 18
HELIX 19 19 VAL A 407 ALA A 420 1 14
HELIX 20 20 PRO A 440 GLY A 444 5 5
HELIX 21 21 GLU A 450 PHE A 455 1 6
HELIX 22 22 GLY A 456 ASP A 460 5 5
HELIX 23 23 THR A 466 GLY A 487 1 22
HELIX 24 24 ARG A 525 ARG A 534 1 10
HELIX 25 25 ARG A 534 SER A 541 1 8
SHEET 1 A 3 LEU A 9 VAL A 12 0
SHEET 2 A 3 GLY A 15 ARG A 18 -1 O LEU A 17 N VAL A 10
SHEET 3 A 3 VAL A 59 ASP A 61 1 O VAL A 60 N ARG A 16
SHEET 1 B11 ILE A 20 LEU A 22 0
SHEET 2 B11 VAL A 29 PRO A 36 -1 O VAL A 29 N LEU A 22
SHEET 3 B11 TYR A 98 PRO A 104 -1 O VAL A 101 N PHE A 32
SHEET 4 B11 VAL A 145 MET A 149 -1 O LEU A 146 N TRP A 102
SHEET 5 B11 THR A 112 ILE A 118 1 N TRP A 117 O VAL A 147
SHEET 6 B11 GLY A 192 GLU A 202 1 O PHE A 200 N VAL A 116
SHEET 7 B11 ARG A 224 GLN A 228 1 O VAL A 226 N LEU A 199
SHEET 8 B11 GLN A 325 VAL A 331 1 O LEU A 327 N ALA A 225
SHEET 9 B11 ARG A 424 PHE A 430 1 O TYR A 426 N VAL A 328
SHEET 10 B11 GLN A 509 LEU A 513 1 O VAL A 511 N VAL A 429
SHEET 11 B11 GLU A 519 ARG A 522 -1 O ARG A 521 N TYR A 510
SHEET 1 C 2 ALA A 38 GLU A 39 0
SHEET 2 C 2 GLU A 51 PRO A 52 -1 O GLU A 51 N GLU A 39
SHEET 1 D 2 VAL A 68 CYS A 69 0
SHEET 2 D 2 LEU A 92 SER A 93 1 O SER A 93 N VAL A 68
SHEET 1 E 2 MET B 2 SER B 5 0
SHEET 2 E 2 ILE B 13 ASN B 16 -1 O ILE B 13 N SER B 5
SHEET 1 F 3 VAL B 34 CYS B 39 0
SHEET 2 F 3 CYS B 22 ARG B 27 -1 N LYS B 25 O GLY B 36
SHEET 3 F 3 LEU B 48 CYS B 53 -1 O GLU B 49 N SER B 26
SSBOND 1 CYS A 69 CYS A 96 1555 1555 2.06
SSBOND 2 CYS A 257 CYS A 272 1555 1555 2.06
SSBOND 3 CYS A 409 CYS A 529 1555 1555 2.07
SSBOND 4 CYS B 3 CYS B 22 1555 1555 2.03
SSBOND 5 CYS B 17 CYS B 39 1555 1555 2.04
SSBOND 6 CYS B 41 CYS B 52 1555 1555 2.05
SSBOND 7 CYS B 53 CYS B 59 1555 1555 2.04
LINK C1 FUC A 605 O6 NAG A 606 1555 1555 1.21
LINK ND2 ASN A 464 C1 NAG A 609 1555 1555 1.48
LINK ND2 ASN A 350 C1 NAG A 606 1555 1555 1.53
LINK O4 NAG A 607 C1 BMA A 608 1555 1555 1.55
LINK O4 NAG A 606 C1 NAG A 607 1555 1555 1.55
CISPEP 1 TYR A 105 PRO A 106 0 3.10
CISPEP 2 PRO A 492 ARG A 493 0 2.85
CISPEP 3 PRO B 30 PRO B 31 0 4.70
CISPEP 4 SER B 55 PRO B 56 0 -5.37
SITE 1 AC1 4 ARG A 525 ALA A 526 GLN A 527 ALA A 528
SITE 1 AC2 3 GLY A 240 MET A 241 GLY A 242
SITE 1 AC3 3 THR A 504 GLY A 506 ALA A 507
SITE 1 AC4 4 ARG A 16 SER A 57 GLY A 58 ARG A 165
SITE 1 AC5 2 SER A 347 NAG A 606
SITE 1 AC6 4 SER A 347 ASN A 350 FUC A 605 NAG A 607
SITE 1 AC7 3 GLY A 345 NAG A 606 BMA A 608
SITE 1 AC8 1 NAG A 607
SITE 1 AC9 2 SER A 462 ASN A 464
CRYST1 151.705 151.705 247.862 90.00 90.00 120.00 H 3 2 18
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 0.006592 0.003806 0.000000 0.00000
SCALE2 0.000000 0.007611 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004035 0.00000
TER 4140 THR A 543
TER 4605 TYR B 61
MASTER 363 0 9 25 23 0 9 6 4719 2 99 47
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