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HEADER HYDROLASE 07-SEP-15 5DLP
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 5DLP 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. 2.70 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) : 2.70
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 96.18
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.5
REMARK 3 NUMBER OF REFLECTIONS : 25658
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) : 0.194
REMARK 3 R VALUE (WORKING SET) : 0.193
REMARK 3 FREE R VALUE : 0.224
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1356
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) : 2.70
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.77
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1889
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 98.50
REMARK 3 BIN R VALUE (WORKING SET) : 0.2700
REMARK 3 BIN FREE R VALUE SET COUNT : 84
REMARK 3 BIN FREE R VALUE : 0.3370
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4179
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 194
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) : 52.02
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.33000
REMARK 3 B22 (A**2) : -0.33000
REMARK 3 B33 (A**2) : 1.06000
REMARK 3 B12 (A**2) : -0.16000
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): 0.391
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.255
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.203
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 22.738
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.944
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.924
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 4493 ; 0.007 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 4035 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 6134 ; 1.201 ; 1.987
REMARK 3 BOND ANGLES OTHERS (DEGREES): 9250 ; 0.731 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 531 ; 5.890 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 200 ;32.203 ;23.950
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 667 ;13.322 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 22 ;14.873 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 672 ; 0.065 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 4996 ; 0.005 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 1062 ; 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 ; 1.162 ; 3.383
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 2126 ; 1.157 ; 3.381
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2657 ; 1.934 ; 5.075
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 2658 ; 1.935 ; 5.076
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2366 ; 1.460 ; 3.775
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 2306 ; 1.400 ; 3.680
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 3388 ; 2.346 ; 5.481
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 5152 ; 4.690 ;28.993
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 5151 ; 4.692 ;28.992
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): -53.8059 36.5123 10.6917
REMARK 3 T TENSOR
REMARK 3 T11: 0.0244 T22: 0.1152
REMARK 3 T33: 0.0078 T12: 0.0265
REMARK 3 T13: 0.0022 T23: -0.0076
REMARK 3 L TENSOR
REMARK 3 L11: 1.3853 L22: 1.4242
REMARK 3 L33: 2.0750 L12: 0.1751
REMARK 3 L13: 0.1981 L23: 0.3648
REMARK 3 S TENSOR
REMARK 3 S11: -0.0061 S12: 0.0922 S13: 0.0539
REMARK 3 S21: 0.0446 S22: -0.0097 S23: 0.0817
REMARK 3 S31: -0.0960 S32: -0.2054 S33: 0.0158
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 5DLP COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 07-SEP-15.
REMARK 100 THE DEPOSITION ID IS D_1000213396.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 07-NOV-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 : SLS
REMARK 200 BEAMLINE : X10SA
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0000
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : PSI PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 27016
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.700
REMARK 200 RESOLUTION RANGE LOW (A) : 96.180
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.9
REMARK 200 DATA REDUNDANCY : 6.400
REMARK 200 R MERGE (I) : 0.10400
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 6.4000
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) : 2.85
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.64300
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: 2W9I
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 69.11
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.98
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 46% PEG200 (V/V) IN 100 MM NACL/1 MM
REMARK 280 MES, PH 6.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 277K
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 45.72400
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 91.44800
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 91.44800
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 45.72400
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: 4260 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 21930 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -150.0 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 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 A 538
REMARK 465 GLY A 539
REMARK 465 GLU A 540
REMARK 465 LEU A 541
REMARK 465 SER A 542
REMARK 465 SER A 543
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 14 CG CD CE NZ
REMARK 470 ARG A 47 CG CD NE CZ NH1 NH2
REMARK 470 GLU A 260 CG CD OE1 OE2
REMARK 470 GLU A 268 CG CD OE1 OE2
REMARK 470 LYS A 270 CG CD CE NZ
REMARK 470 ARG A 349 CG CD NE CZ NH1 NH2
REMARK 470 GLU A 350 CG CD OE1 OE2
REMARK 470 LYS A 357 CE NZ
REMARK 470 GLU A 455 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 491 CD CE NZ
REMARK 470 GLU A 508 CG CD OE1 OE2
REMARK 470 LYS A 511 CG CD CE NZ
REMARK 470 GLN A 526 CD 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 LEU A 23 51.23 36.06
REMARK 500 PHE A 45 -17.71 78.81
REMARK 500 PRO A 53 156.30 -49.88
REMARK 500 SER A 108 86.29 -161.17
REMARK 500 PHE A 120 -0.37 67.65
REMARK 500 LEU A 158 79.72 -105.11
REMARK 500 SER A 200 -124.14 59.42
REMARK 500 GLU A 299 -67.92 -109.85
REMARK 500 THR A 317 -162.96 -160.10
REMARK 500 VAL A 400 -62.59 -131.87
REMARK 500 SER A 487 129.58 -17.10
REMARK 500 LEU A 516 109.35 -57.23
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 MBT A 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 610
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 611
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 612
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 613
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 614
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 615
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 616
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 617
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 618
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 619
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 620
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 621
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 622
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 623
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 624
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG A
REMARK 800 602 through FUC A 603 bound to ASN A 59
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG A 604 bound
REMARK 800 to ASN A 416
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG A
REMARK 800 605 through MAN A 609 bound to ASN A 457
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2W9I RELATED DB: PDB
REMARK 900 RELATED ID: 1W6R RELATED DB: PDB
DBREF 5DLP A 1 543 UNP P04058 ACES_TORCA 22 564
SEQRES 1 A 543 ASP ASP HIS SER GLU LEU LEU VAL ASN THR LYS SER GLY
SEQRES 2 A 543 LYS VAL MET GLY THR ARG VAL PRO VAL LEU SER SER HIS
SEQRES 3 A 543 ILE SER ALA PHE LEU GLY ILE PRO PHE ALA GLU PRO PRO
SEQRES 4 A 543 VAL GLY ASN MET ARG PHE ARG ARG PRO GLU PRO LYS LYS
SEQRES 5 A 543 PRO TRP SER GLY VAL TRP ASN ALA SER THR TYR PRO ASN
SEQRES 6 A 543 ASN CYS GLN GLN TYR VAL ASP GLU GLN PHE PRO GLY PHE
SEQRES 7 A 543 SER GLY SER GLU MET TRP ASN PRO ASN ARG GLU MET SER
SEQRES 8 A 543 GLU ASP CYS LEU TYR LEU ASN ILE TRP VAL PRO SER PRO
SEQRES 9 A 543 ARG PRO LYS SER THR THR VAL MET VAL TRP ILE TYR GLY
SEQRES 10 A 543 GLY GLY PHE TYR SER GLY SER SER THR LEU ASP VAL TYR
SEQRES 11 A 543 ASN GLY LYS TYR LEU ALA TYR THR GLU GLU VAL VAL LEU
SEQRES 12 A 543 VAL SER LEU SER TYR ARG VAL GLY ALA PHE GLY PHE LEU
SEQRES 13 A 543 ALA LEU HIS GLY SER GLN GLU ALA PRO GLY ASN VAL GLY
SEQRES 14 A 543 LEU LEU ASP GLN ARG MET ALA LEU GLN TRP VAL HIS ASP
SEQRES 15 A 543 ASN ILE GLN PHE PHE GLY GLY ASP PRO LYS THR VAL THR
SEQRES 16 A 543 ILE PHE GLY GLU SER ALA GLY GLY ALA SER VAL GLY MET
SEQRES 17 A 543 HIS ILE LEU SER PRO GLY SER ARG ASP LEU PHE ARG ARG
SEQRES 18 A 543 ALA ILE LEU GLN SER GLY SER PRO ASN CYS PRO TRP ALA
SEQRES 19 A 543 SER VAL SER VAL ALA GLU GLY ARG ARG ARG ALA VAL GLU
SEQRES 20 A 543 LEU GLY ARG ASN LEU ASN CYS ASN LEU ASN SER ASP GLU
SEQRES 21 A 543 GLU LEU ILE HIS CYS LEU ARG GLU LYS LYS PRO GLN GLU
SEQRES 22 A 543 LEU ILE ASP VAL GLU TRP ASN VAL LEU PRO PHE ASP SER
SEQRES 23 A 543 ILE PHE ARG PHE SER PHE VAL PRO VAL ILE ASP GLY GLU
SEQRES 24 A 543 PHE PHE PRO THR SER LEU GLU SER MET LEU ASN SER GLY
SEQRES 25 A 543 ASN PHE LYS LYS THR GLN ILE LEU LEU GLY VAL ASN LYS
SEQRES 26 A 543 ASP GLU GLY SER PHE PHE LEU LEU TYR GLY ALA PRO GLY
SEQRES 27 A 543 PHE SER LYS ASP SER GLU SER LYS ILE SER ARG GLU ASP
SEQRES 28 A 543 PHE MET SER GLY VAL LYS LEU SER VAL PRO HIS ALA ASN
SEQRES 29 A 543 ASP LEU GLY LEU ASP ALA VAL THR LEU GLN TYR THR ASP
SEQRES 30 A 543 TRP MET ASP ASP ASN ASN GLY ILE LYS ASN ARG ASP GLY
SEQRES 31 A 543 LEU ASP ASP ILE VAL GLY ASP HIS ASN VAL ILE CYS PRO
SEQRES 32 A 543 LEU MET HIS PHE VAL ASN LYS TYR THR LYS PHE GLY ASN
SEQRES 33 A 543 GLY THR TYR LEU TYR PHE PHE ASN HIS ARG ALA SER ASN
SEQRES 34 A 543 LEU VAL TRP PRO GLU TRP MET GLY VAL ILE HIS GLY TYR
SEQRES 35 A 543 GLU ILE GLU PHE VAL PHE GLY LEU PRO LEU VAL LYS GLU
SEQRES 36 A 543 LEU ASN TYR THR ALA GLU GLU GLU ALA LEU SER ARG ARG
SEQRES 37 A 543 ILE MET HIS TYR TRP ALA THR PHE ALA LYS THR GLY ASN
SEQRES 38 A 543 PRO ASN GLU PRO HIS SER GLN GLU SER LYS TRP PRO LEU
SEQRES 39 A 543 PHE THR THR LYS GLU GLN LYS PHE ILE ASP LEU ASN THR
SEQRES 40 A 543 GLU PRO MET LYS VAL HIS GLN ARG LEU ARG VAL GLN MET
SEQRES 41 A 543 CYS VAL PHE TRP ASN GLN PHE LEU PRO LYS LEU LEU ASN
SEQRES 42 A 543 ALA THR ALA CYS ASP GLY GLU LEU SER SER
HET MBT A 601 20
HET NAG A 602 14
HET FUC A 603 10
HET NAG A 604 14
HET NAG A 605 14
HET NAG A 606 14
HET BMA A 607 11
HET MAN A 608 11
HET MAN A 609 11
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
HET SO4 A 619 5
HET SO4 A 620 5
HET SO4 A 621 5
HET SO4 A 622 5
HET SO4 A 623 5
HET SO4 A 624 5
HETNAM MBT 3,7-BIS(DIMETHYLAMINO)PHENOTHIAZIN-5-IUM
HETNAM NAG N-ACETYL-D-GLUCOSAMINE
HETNAM FUC ALPHA-L-FUCOSE
HETNAM BMA BETA-D-MANNOSE
HETNAM MAN ALPHA-D-MANNOSE
HETNAM SO4 SULFATE ION
HETSYN MBT METHYLENE BLUE
FORMUL 2 MBT C16 H18 N3 S 1+
FORMUL 3 NAG 4(C8 H15 N O6)
FORMUL 3 FUC C6 H12 O5
FORMUL 5 BMA C6 H12 O6
FORMUL 5 MAN 2(C6 H12 O6)
FORMUL 6 SO4 15(O4 S 2-)
FORMUL 21 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 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 ASP A 276 1 7
HELIX 13 AB4 VAL A 277 LEU A 282 5 6
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 THR A 376 1 13
HELIX 18 AB9 ASP A 377 ASP A 381 5 5
HELIX 19 AC1 ASN A 383 VAL A 400 1 18
HELIX 20 AC2 VAL A 400 LYS A 413 1 14
HELIX 21 AC3 PRO A 433 GLY A 437 5 5
HELIX 22 AC4 GLU A 443 PHE A 448 1 6
HELIX 23 AC5 GLY A 449 ASN A 457 5 9
HELIX 24 AC6 THR A 459 GLY A 480 1 22
HELIX 25 AC7 ARG A 517 GLN A 526 1 10
HELIX 26 AC8 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 VAL A 22 0
SHEET 2 AA211 SER A 25 PRO A 34 -1 O ALA A 29 N THR A 18
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 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 PHE A 423 N VAL A 323
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 2.04
SSBOND 2 CYS A 254 CYS A 265 1555 1555 2.03
SSBOND 3 CYS A 402 CYS A 521 1555 1555 2.04
LINK ND2 ASN A 59 C1 NAG A 602 1555 1555 1.46
LINK ND2 ASN A 416 C1 NAG A 604 1555 1555 1.45
LINK ND2 ASN A 457 C1 NAG A 605 1555 1555 1.46
LINK O6 NAG A 602 C1 FUC A 603 1555 1555 1.45
LINK O4 NAG A 605 C1 NAG A 606 1555 1555 1.45
LINK O4 NAG A 606 C1 BMA A 607 1555 1555 1.45
LINK O3 BMA A 607 C1 MAN A 608 1555 1555 1.46
LINK O2 MAN A 608 C1 MAN A 609 1555 1555 1.45
CISPEP 1 SER A 103 PRO A 104 0 -1.33
SITE 1 AC1 7 TYR A 70 TYR A 121 TRP A 279 PHE A 330
SITE 2 AC1 7 PHE A 331 TYR A 334 HOH A 702
SITE 1 AC2 2 SER A 237 ARG A 243
SITE 1 AC3 2 LYS A 346 GLY A 384
SITE 1 AC4 3 MET A 379 HIS A 513 GLN A 514
SITE 1 AC5 4 PRO A 106 LYS A 107 SER A 108 THR A 109
SITE 1 AC6 3 HIS A 406 ASN A 525 GLN A 526
SITE 1 AC7 5 ASN A 424 HIS A 425 ASN A 506 THR A 507
SITE 2 AC7 5 GLU A 508
SITE 1 AC8 3 THR A 459 ALA A 460 GLU A 461
SITE 1 AC9 4 VAL A 22 LEU A 23 LYS A 133 TYR A 134
SITE 1 AD1 5 ARG A 289 VAL A 360 PRO A 361 HIS A 362
SITE 2 AD1 5 HIS A 398
SITE 1 AD2 2 PRO A 433 GLU A 434
SITE 1 AD3 3 GLN A 68 SER A 91 GLU A 92
SITE 1 AD4 3 PRO A 213 SER A 343 GLU A 344
SITE 1 AD5 2 SER A 490 LYS A 491
SITE 1 AD6 5 PRO A 76 ARG A 220 ARG A 221 GLN A 318
SITE 2 AD6 5 ASN A 416
SITE 1 AD7 3 ARG A 46 GLN A 162 ASN A 382
SITE 1 AD8 2 ASN A 59 SER A 61
SITE 1 AD9 2 ASN A 416 MAN A 609
SITE 1 AE1 5 LYS A 413 PHE A 414 GLU A 455 ASN A 457
SITE 2 AE1 5 NAG A 604
CRYST1 111.059 111.059 137.172 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 0.009004 0.005199 0.000000 0.00000
SCALE2 0.000000 0.010397 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007290 0.00000
TER 4180 THR A 535
MASTER 418 0 24 26 14 0 24 6 4388 1 203 42
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