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HEADER HYDROLASE 06-OCT-15 5E4J
TITLE ACETYCHOLINESTERASE METHYLENE BLUE NO PEG
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ACETYLCHOLINESTERASE;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: ACHE;
COMPND 5 EC: 3.1.1.7
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: TORPEDO CALIFORNICA;
SOURCE 3 ORGANISM_COMMON: PACIFIC ELECTRIC RAY;
SOURCE 4 ORGANISM_TAXID: 7787
KEYWDS INHIBITOR, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR O.DYM
REVDAT 1 30-MAR-16 5E4J 0
JRNL AUTH O.DYM,W.SONG,C.FELDER,E.ROTH,V.SHNYROV,Y.ASHANI,Y.XU,
JRNL AUTH 2 R.P.JOOSTEN,L.WEINER,J.L.SUSSMAN,I.SILMAN
JRNL TITL THE IMPACT OF CRYSTALLIZATION CONDITIONS ON STRUCTURE-BASED
JRNL TITL 2 DRUG DESIGN: A CASE STUDY ON THE METHYLENE
JRNL TITL 3 BLUE/ACETYLCHOLINESTERASE COMPLEX.
JRNL REF PROTEIN SCI. 2016
JRNL REFN ESSN 1469-896X
JRNL PMID 26990888
JRNL DOI 10.1002/PRO.2923
REMARK 2
REMARK 2 RESOLUTION. 2.54 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0073
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.54
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 48.15
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 3 NUMBER OF REFLECTIONS : 31097
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING + TEST SET) : 0.193
REMARK 3 R VALUE (WORKING SET) : 0.191
REMARK 3 FREE R VALUE : 0.229
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 1656
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.54
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.61
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2241
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 100.0
REMARK 3 BIN R VALUE (WORKING SET) : 0.3060
REMARK 3 BIN FREE R VALUE SET COUNT : 124
REMARK 3 BIN FREE R VALUE : 0.3650
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4174
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 157
REMARK 3 SOLVENT ATOMS : 15
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 59.39
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.67000
REMARK 3 B22 (A**2) : -0.67000
REMARK 3 B33 (A**2) : 2.18000
REMARK 3 B12 (A**2) : -0.34000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.280
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.222
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.188
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 19.863
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.952
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.931
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 4456 ; 0.007 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 4059 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 6072 ; 1.391 ; 1.977
REMARK 3 BOND ANGLES OTHERS (DEGREES): 9314 ; 0.778 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 531 ; 6.060 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 196 ;32.710 ;23.827
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 674 ;15.703 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 22 ;17.151 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 664 ; 0.164 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 4956 ; 0.005 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 1056 ; 0.001 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 2127 ; 1.262 ; 3.256
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 2126 ; 1.257 ; 3.255
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2657 ; 2.133 ; 4.884
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 2658 ; 2.135 ; 4.885
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2329 ; 1.537 ; 3.547
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 2290 ; 1.499 ; 3.486
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 3356 ; 2.455 ; 5.172
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 4953 ; 4.436 ;26.388
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 4953 ; 4.434 ;26.392
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 1
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 4 A 535
REMARK 3 ORIGIN FOR THE GROUP (A): 52.5861 -28.2562 33.2983
REMARK 3 T TENSOR
REMARK 3 T11: 0.0921 T22: 0.2315
REMARK 3 T33: 0.0072 T12: -0.1046
REMARK 3 T13: 0.0160 T23: -0.0169
REMARK 3 L TENSOR
REMARK 3 L11: 1.4683 L22: 2.1497
REMARK 3 L33: 3.0133 L12: -0.0876
REMARK 3 L13: -0.4228 L23: 0.6247
REMARK 3 S TENSOR
REMARK 3 S11: -0.1937 S12: -0.0531 S13: -0.0587
REMARK 3 S21: -0.1185 S22: 0.1274 S23: 0.0709
REMARK 3 S31: 0.2129 S32: -0.3271 S33: 0.0664
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 5E4J COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 06-OCT-15.
REMARK 100 THE DEPOSITION ID IS D_1000214251.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 20-SEP-12
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.5
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) : 0.9763
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 38533
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.540
REMARK 200 RESOLUTION RANGE LOW (A) : 48.150
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 200 DATA REDUNDANCY : 6.900
REMARK 200 R MERGE (I) : 0.14600
REMARK 200 R SYM (I) : 0.14000
REMARK 200 FOR THE DATA SET : 3.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.54
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.68
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.8
REMARK 200 DATA REDUNDANCY IN SHELL : 7.10
REMARK 200 R MERGE FOR SHELL (I) : 0.56000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 1.200
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 (%): 69.83
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.08
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 60% AS/360 MM NA,K PHOSPHATE/100 MM NA
REMARK 280 PHOSPHATE, PH 6.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE
REMARK 280 279K
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 45.67667
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 91.35333
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 91.35333
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 45.67667
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: 3540 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 21340 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -104.0 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 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 52 CE NZ
REMARK 470 GLU A 140 CG CD OE1 OE2
REMARK 470 ARG A 250 CZ NH1 NH2
REMARK 470 GLU A 260 CG CD OE1 OE2
REMARK 470 GLU A 261 CG CD OE1 OE2
REMARK 470 GLU A 268 OE1 OE2
REMARK 470 LYS A 270 CG CD CE NZ
REMARK 470 GLU A 344 OE1 OE2
REMARK 470 GLU A 350 OE1 OE2
REMARK 470 GLU A 434 CG CD OE1 OE2
REMARK 470 LYS A 454 CD CE NZ
REMARK 470 GLU A 455 CG CD OE1 OE2
REMARK 470 GLU A 461 CD OE1 OE2
REMARK 470 HIS A 486 CG ND1 CD2 CE1 NE2
REMARK 470 SER A 487 OG
REMARK 470 GLN A 488 CG CD OE1 NE2
REMARK 470 GLU A 489 CG CD OE1 OE2
REMARK 470 LYS A 498 CG CD CE NZ
REMARK 470 GLU A 508 CD OE1 OE2
REMARK 470 LYS A 511 CD CE NZ
REMARK 470 ARG A 515 CZ NH1 NH2
REMARK 470 GLN A 526 OE1 NE2
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 -7.82 77.67
REMARK 500 PHE A 120 2.98 59.09
REMARK 500 LEU A 158 76.58 -104.83
REMARK 500 ALA A 164 65.51 -150.18
REMARK 500 SER A 200 -118.24 68.04
REMARK 500 GLU A 299 -74.22 -82.64
REMARK 500 THR A 317 -157.57 -153.89
REMARK 500 ASP A 380 -70.00 -87.68
REMARK 500 ASP A 381 -45.84 80.51
REMARK 500 VAL A 400 -60.81 -133.37
REMARK 500 HIS A 486 -96.52 -88.26
REMARK 500 SER A 487 113.72 57.33
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 DME A 608
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 609
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 610
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 611
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 612
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 613
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 614
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 615
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 616
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 617
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 618
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD3
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: AD4
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: AD5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG A
REMARK 800 603 through MAN A 607 bound to ASN A 457
DBREF 5E4J A 4 535 UNP P04058 ACES_TORCA 25 556
SEQRES 1 A 532 SER GLU LEU LEU VAL ASN THR LYS SER GLY LYS VAL MET
SEQRES 2 A 532 GLY THR ARG VAL PRO VAL LEU SER SER HIS ILE SER ALA
SEQRES 3 A 532 PHE LEU GLY ILE PRO PHE ALA GLU PRO PRO VAL GLY ASN
SEQRES 4 A 532 MET ARG PHE ARG ARG PRO GLU PRO LYS LYS PRO TRP SER
SEQRES 5 A 532 GLY VAL TRP ASN ALA SER THR TYR PRO ASN ASN CYS GLN
SEQRES 6 A 532 GLN TYR VAL ASP GLU GLN PHE PRO GLY PHE SER GLY SER
SEQRES 7 A 532 GLU MET TRP ASN PRO ASN ARG GLU MET SER GLU ASP CYS
SEQRES 8 A 532 LEU TYR LEU ASN ILE TRP VAL PRO SER PRO ARG PRO LYS
SEQRES 9 A 532 SER THR THR VAL MET VAL TRP ILE TYR GLY GLY GLY PHE
SEQRES 10 A 532 TYR SER GLY SER SER THR LEU ASP VAL TYR ASN GLY LYS
SEQRES 11 A 532 TYR LEU ALA TYR THR GLU GLU VAL VAL LEU VAL SER LEU
SEQRES 12 A 532 SER TYR ARG VAL GLY ALA PHE GLY PHE LEU ALA LEU HIS
SEQRES 13 A 532 GLY SER GLN GLU ALA PRO GLY ASN VAL GLY LEU LEU ASP
SEQRES 14 A 532 GLN ARG MET ALA LEU GLN TRP VAL HIS ASP ASN ILE GLN
SEQRES 15 A 532 PHE PHE GLY GLY ASP PRO LYS THR VAL THR ILE PHE GLY
SEQRES 16 A 532 GLU SER ALA GLY GLY ALA SER VAL GLY MET HIS ILE LEU
SEQRES 17 A 532 SER PRO GLY SER ARG ASP LEU PHE ARG ARG ALA ILE LEU
SEQRES 18 A 532 GLN SER GLY SER PRO ASN CYS PRO TRP ALA SER VAL SER
SEQRES 19 A 532 VAL ALA GLU GLY ARG ARG ARG ALA VAL GLU LEU GLY ARG
SEQRES 20 A 532 ASN LEU ASN CYS ASN LEU ASN SER ASP GLU GLU LEU ILE
SEQRES 21 A 532 HIS CYS LEU ARG GLU LYS LYS PRO GLN GLU LEU ILE ASP
SEQRES 22 A 532 VAL GLU TRP ASN VAL LEU PRO PHE ASP SER ILE PHE ARG
SEQRES 23 A 532 PHE SER PHE VAL PRO VAL ILE ASP GLY GLU PHE PHE PRO
SEQRES 24 A 532 THR SER LEU GLU SER MET LEU ASN SER GLY ASN PHE LYS
SEQRES 25 A 532 LYS THR GLN ILE LEU LEU GLY VAL ASN LYS ASP GLU GLY
SEQRES 26 A 532 SER PHE PHE LEU LEU TYR GLY ALA PRO GLY PHE SER LYS
SEQRES 27 A 532 ASP SER GLU SER LYS ILE SER ARG GLU ASP PHE MET SER
SEQRES 28 A 532 GLY VAL LYS LEU SER VAL PRO HIS ALA ASN ASP LEU GLY
SEQRES 29 A 532 LEU ASP ALA VAL THR LEU GLN TYR THR ASP TRP MET ASP
SEQRES 30 A 532 ASP ASN ASN GLY ILE LYS ASN ARG ASP GLY LEU ASP ASP
SEQRES 31 A 532 ILE VAL GLY ASP HIS ASN VAL ILE CYS PRO LEU MET HIS
SEQRES 32 A 532 PHE VAL ASN LYS TYR THR LYS PHE GLY ASN GLY THR TYR
SEQRES 33 A 532 LEU TYR PHE PHE ASN HIS ARG ALA SER ASN LEU VAL TRP
SEQRES 34 A 532 PRO GLU TRP MET GLY VAL ILE HIS GLY TYR GLU ILE GLU
SEQRES 35 A 532 PHE VAL PHE GLY LEU PRO LEU VAL LYS GLU LEU ASN TYR
SEQRES 36 A 532 THR ALA GLU GLU GLU ALA LEU SER ARG ARG ILE MET HIS
SEQRES 37 A 532 TYR TRP ALA THR PHE ALA LYS THR GLY ASN PRO ASN GLU
SEQRES 38 A 532 PRO HIS SER GLN GLU SER LYS TRP PRO LEU PHE THR THR
SEQRES 39 A 532 LYS GLU GLN LYS PHE ILE ASP LEU ASN THR GLU PRO MET
SEQRES 40 A 532 LYS VAL HIS GLN ARG LEU ARG VAL GLN MET CYS VAL PHE
SEQRES 41 A 532 TRP ASN GLN PHE LEU PRO LYS LEU LEU ASN ALA THR
HET NAG A 601 14
HET NAG A 602 14
HET NAG A 603 14
HET NAG A 604 14
HET BMA A 605 11
HET MAN A 606 11
HET MAN A 607 11
HET DME A 608 18
HET SO4 A 609 5
HET SO4 A 610 5
HET SO4 A 611 5
HET SO4 A 612 5
HET SO4 A 613 5
HET SO4 A 614 5
HET SO4 A 615 5
HET SO4 A 616 5
HET SO4 A 617 5
HET SO4 A 618 5
HETNAM NAG N-ACETYL-D-GLUCOSAMINE
HETNAM BMA BETA-D-MANNOSE
HETNAM MAN ALPHA-D-MANNOSE
HETNAM DME DECAMETHONIUM ION
HETNAM SO4 SULFATE ION
FORMUL 2 NAG 4(C8 H15 N O6)
FORMUL 4 BMA C6 H12 O6
FORMUL 4 MAN 2(C6 H12 O6)
FORMUL 5 DME C16 H38 N2 2+
FORMUL 6 SO4 10(O4 S 2-)
FORMUL 16 HOH *15(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 215 PHE A 219 5 5
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 GLY A 415 1 16
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
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 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 VAL A 101 N SER A 28
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 GLN A 318 ASN A 324 1 O LEU A 320 N LEU A 224
SHEET 9 AA211 GLY A 417 PHE A 423 1 O GLY A 417 N ILE A 319
SHEET 10 AA211 LYS A 501 LEU A 505 1 O ILE A 503 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 67 CYS A 94 1555 1555 2.06
SSBOND 2 CYS A 254 CYS A 265 1555 1555 2.07
SSBOND 3 CYS A 402 CYS A 521 1555 1555 2.08
LINK ND2 ASN A 59 C1 NAG A 601 1555 1555 1.46
LINK ND2 ASN A 416 C1 NAG A 602 1555 1555 1.46
LINK ND2 ASN A 457 C1 NAG A 603 1555 1555 1.47
LINK O4 NAG A 603 C1 NAG A 604 1555 1555 1.45
LINK O4 NAG A 604 C1 BMA A 605 1555 1555 1.45
LINK O3 BMA A 605 C1 MAN A 606 1555 1555 1.45
LINK O2 MAN A 606 C1 MAN A 607 1555 1555 1.44
CISPEP 1 SER A 103 PRO A 104 0 -1.83
SITE 1 AC1 8 TYR A 70 TRP A 84 GLY A 118 TYR A 121
SITE 2 AC1 8 GLU A 199 TRP A 279 TYR A 334 GLY A 441
SITE 1 AC2 3 HIS A 406 ASN A 525 GLN A 526
SITE 1 AC3 5 ASN A 424 HIS A 425 ASN A 506 THR A 507
SITE 2 AC3 5 GLU A 508
SITE 1 AC4 5 PRO A 21 VAL A 22 LEU A 23 LYS A 133
SITE 2 AC4 5 TYR A 134
SITE 1 AC5 6 ARG A 289 SER A 359 VAL A 360 PRO A 361
SITE 2 AC5 6 HIS A 362 HIS A 398
SITE 1 AC6 4 SER A 237 ALA A 239 GLU A 240 ARG A 243
SITE 1 AC7 2 HIS A 513 GLN A 514
SITE 1 AC8 3 LYS A 346 ASN A 382 GLY A 384
SITE 1 AC9 2 SER A 258 ASP A 259
SITE 1 AD1 4 GLN A 68 SER A 91 GLU A 92 PRO A 271
SITE 1 AD2 5 PRO A 213 PRO A 302 ASP A 342 SER A 343
SITE 2 AD2 5 GLU A 344
SITE 1 AD3 2 ASN A 59 SER A 61
SITE 1 AD4 2 ASN A 416 MAN A 607
SITE 1 AD5 5 LYS A 413 PHE A 414 GLY A 415 ASN A 457
SITE 2 AD5 5 NAG A 602
CRYST1 111.210 111.210 137.030 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 0.008992 0.005192 0.000000 0.00000
SCALE2 0.000000 0.010383 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007298 0.00000
TER 4175 THR A 535
MASTER 382 0 18 25 14 0 20 6 4346 1 166 41
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