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HEADER HYDROLASE 20-AUG-14 4W63
TITLE TORPEDO CALIFORNICA ACETYLCHOLINESTERASE IN COMPLEX WITH A TACRINE-
TITLE 2 BENZOFURAN HYBRID INHIBITOR
CAVEAT 4W63 NAG A 604 HAS WRONG CHIRALITY AT ATOM C1
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 MULTITARGET DRUG, ENZYME-INHIBITOR COMPLEX, TACRINE, BENZOFURAN,
KEYWDS 2 HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR A.PESARESI,S.SAMEZ,D.LAMBA
REVDAT 1 09-SEP-15 4W63 0
JRNL AUTH A.PESARESI,S.SAMEZ,D.LAMBA
JRNL TITL TORPEDO CALIFORNICA ACETYLCHOLINESTERASE IN COMPLEX WITH A
JRNL TITL 2 TACRINE-BENZOFURAN HYBRID INHIBITOR
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.80 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.7.0032
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) : 2.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 45.90
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 89.6
REMARK 3 NUMBER OF REFLECTIONS : 21631
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) : 0.195
REMARK 3 R VALUE (WORKING SET) : 0.192
REMARK 3 FREE R VALUE : 0.260
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1132
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) : 2.80
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.87
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1630
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 90.68
REMARK 3 BIN R VALUE (WORKING SET) : 0.3560
REMARK 3 BIN FREE R VALUE SET COUNT : 63
REMARK 3 BIN FREE R VALUE : 0.4640
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4263
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 89
REMARK 3 SOLVENT ATOMS : 95
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 58.79
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 1.17000
REMARK 3 B22 (A**2) : 1.17000
REMARK 3 B33 (A**2) : -3.79000
REMARK 3 B12 (A**2) : 1.17000
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): 0.600
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.347
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.224
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 11.520
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.944
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.897
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 4460 ; 0.013 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 4070 ; 0.003 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 6067 ; 1.786 ; 1.967
REMARK 3 BOND ANGLES OTHERS (DEGREES): 9333 ; 0.952 ; 3.004
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 533 ; 7.320 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 209 ;35.319 ;23.971
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 683 ;17.482 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 24 ;16.921 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 639 ; 0.094 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 5065 ; 0.007 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 1081 ; 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): 2135 ; 4.516 ; 5.815
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 2134 ; 4.515 ; 5.813
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2667 ; 6.752 ; 8.719
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 2668 ; 6.752 ; 8.721
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2325 ; 4.492 ; 6.168
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 2326 ; 4.491 ; 6.167
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 3401 ; 6.944 ; 9.130
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 5357 ; 9.705 ;47.266
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 5355 ; 9.704 ;47.268
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 : NULL
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 4W63 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 21-AUG-14.
REMARK 100 THE DEPOSITION ID IS D_1000203070.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 16-FEB-14
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.0
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ELETTRA
REMARK 200 BEAMLINE : 5.2R
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 2M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM 7.0.7
REMARK 200 DATA SCALING SOFTWARE : SCALA 3.3.2.1
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 22808
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.800
REMARK 200 RESOLUTION RANGE LOW (A) : 46.220
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 90.0
REMARK 200 DATA REDUNDANCY : 5.000
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 11.7000
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) : 2.95
REMARK 200 COMPLETENESS FOR SHELL (%) : 90.8
REMARK 200 DATA REDUNDANCY IN SHELL : 5.10
REMARK 200 R MERGE FOR SHELL (I) : 0.38600
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 3.400
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER 2.3.0
REMARK 200 STARTING MODEL: 1EA5
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 70.53
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.17
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 30% PRG200, 100MM MES, PH 6.0, VAPOR
REMARK 280 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 46.24000
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 92.48000
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 92.48000
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 46.24000
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: 680 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 21510 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 10.0 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 480
REMARK 480 ZERO OCCUPANCY ATOM
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 480 M RES C SSEQI ATOMS
REMARK 480 ASP A 2 CB CG OD1 OD2
REMARK 480 HIS A 3 CB CG ND1 CD2 CE1 NE2
REMARK 480 LYS A 192 CB CG CD CE NZ
REMARK 480 ASN A 253 OD1 ND2
REMARK 480 LYS A 269 CG CD CE NZ
REMARK 480 SER A 286 CB OG
REMARK 480 ILE A 287 CD1
REMARK 480 LYS A 413 CD CE NZ
REMARK 480 LYS A 454 CE NZ
REMARK 480 GLN A 488 CG CD OE1 NE2
REMARK 480 LYS A 498 CD CE NZ
REMARK 480 LYS A 511 CD CE NZ
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 O SER A 286 O HOH A 701 2.17
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
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 RES CSSEQI ATM2 DEVIATION
REMARK 500 LYS A 192 CA LYS A 192 CB -0.182
REMARK 500 SER A 286 CA SER A 286 CB 0.161
REMARK 500 LYS A 454 CD LYS A 454 CE -0.239
REMARK 500 LYS A 498 CG LYS A 498 CD -0.286
REMARK 500 LYS A 511 CG LYS A 511 CD -0.343
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 HIS A 486 CB - CA - C ANGL. DEV. = -21.9 DEGREES
REMARK 500 GLN A 488 CB - CG - CD ANGL. DEV. = 18.2 DEGREES
REMARK 500 VAL A 518 CB - CA - C ANGL. DEV. = -11.4 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 HIS A 3 18.38 48.25
REMARK 500 LYS A 11 -19.58 -49.10
REMARK 500 SER A 24 -1.09 64.72
REMARK 500 SER A 25 -161.74 -106.52
REMARK 500 ALA A 60 49.88 -102.83
REMARK 500 CYS A 94 -0.46 -148.01
REMARK 500 LYS A 107 -78.81 -88.57
REMARK 500 SER A 200 -130.51 66.99
REMARK 500 ASN A 253 70.51 49.49
REMARK 500 PHE A 284 89.45 156.65
REMARK 500 ASP A 285 -51.49 -170.26
REMARK 500 SER A 286 153.93 74.98
REMARK 500 PHE A 288 162.57 79.32
REMARK 500 ARG A 289 57.45 -113.64
REMARK 500 GLU A 299 -87.65 -109.24
REMARK 500 THR A 303 -168.12 -129.39
REMARK 500 ASN A 313 76.84 -67.46
REMARK 500 GLU A 344 -9.50 -57.64
REMARK 500 ASP A 380 55.63 -179.29
REMARK 500 VAL A 400 -55.45 -132.28
REMARK 500 HIS A 440 109.23 -46.53
REMARK 500 LEU A 450 -36.25 -33.63
REMARK 500 PRO A 485 113.82 -37.94
REMARK 500 HIS A 486 20.82 44.44
REMARK 500 ARG A 515 71.71 43.20
REMARK 500 GLN A 526 -57.57 -126.16
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 PHE A 288 ARG A 289 -125.62
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 HTB A 605
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
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: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG A
REMARK 800 602 through NAG A 603 bound to ASN A 416
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG A 604 bound
REMARK 800 to ASN A 457
DBREF 4W63 A 2 535 UNP P04058 ACES_TORCA 23 556
SEQRES 1 A 534 ASP HIS SER GLU LEU LEU VAL ASN THR LYS SER GLY LYS
SEQRES 2 A 534 VAL MET GLY THR ARG VAL PRO VAL LEU SER SER HIS ILE
SEQRES 3 A 534 SER ALA PHE LEU GLY ILE PRO PHE ALA GLU PRO PRO VAL
SEQRES 4 A 534 GLY ASN MET ARG PHE ARG ARG PRO GLU PRO LYS LYS PRO
SEQRES 5 A 534 TRP SER GLY VAL TRP ASN ALA SER THR TYR PRO ASN ASN
SEQRES 6 A 534 CYS GLN GLN TYR VAL ASP GLU GLN PHE PRO GLY PHE SER
SEQRES 7 A 534 GLY SER GLU MET TRP ASN PRO ASN ARG GLU MET SER GLU
SEQRES 8 A 534 ASP CYS LEU TYR LEU ASN ILE TRP VAL PRO SER PRO ARG
SEQRES 9 A 534 PRO LYS SER THR THR VAL MET VAL TRP ILE TYR GLY GLY
SEQRES 10 A 534 GLY PHE TYR SER GLY SER SER THR LEU ASP VAL TYR ASN
SEQRES 11 A 534 GLY LYS TYR LEU ALA TYR THR GLU GLU VAL VAL LEU VAL
SEQRES 12 A 534 SER LEU SER TYR ARG VAL GLY ALA PHE GLY PHE LEU ALA
SEQRES 13 A 534 LEU HIS GLY SER GLN GLU ALA PRO GLY ASN VAL GLY LEU
SEQRES 14 A 534 LEU ASP GLN ARG MET ALA LEU GLN TRP VAL HIS ASP ASN
SEQRES 15 A 534 ILE GLN PHE PHE GLY GLY ASP PRO LYS THR VAL THR ILE
SEQRES 16 A 534 PHE GLY GLU SER ALA GLY GLY ALA SER VAL GLY MET HIS
SEQRES 17 A 534 ILE LEU SER PRO GLY SER ARG ASP LEU PHE ARG ARG ALA
SEQRES 18 A 534 ILE LEU GLN SER GLY SER PRO ASN CYS PRO TRP ALA SER
SEQRES 19 A 534 VAL SER VAL ALA GLU GLY ARG ARG ARG ALA VAL GLU LEU
SEQRES 20 A 534 GLY ARG ASN LEU ASN CYS ASN LEU ASN SER ASP GLU GLU
SEQRES 21 A 534 LEU ILE HIS CYS LEU ARG GLU LYS LYS PRO GLN GLU LEU
SEQRES 22 A 534 ILE ASP VAL GLU TRP ASN VAL LEU PRO PHE ASP SER ILE
SEQRES 23 A 534 PHE ARG PHE SER PHE VAL PRO VAL ILE ASP GLY GLU PHE
SEQRES 24 A 534 PHE PRO THR SER LEU GLU SER MET LEU ASN SER GLY ASN
SEQRES 25 A 534 PHE LYS LYS THR GLN ILE LEU LEU GLY VAL ASN LYS ASP
SEQRES 26 A 534 GLU GLY SER PHE PHE LEU LEU TYR GLY ALA PRO GLY PHE
SEQRES 27 A 534 SER LYS ASP SER GLU SER LYS ILE SER ARG GLU ASP PHE
SEQRES 28 A 534 MET SER GLY VAL LYS LEU SER VAL PRO HIS ALA ASN ASP
SEQRES 29 A 534 LEU GLY LEU ASP ALA VAL THR LEU GLN TYR THR ASP TRP
SEQRES 30 A 534 MET ASP ASP ASN ASN GLY ILE LYS ASN ARG ASP GLY LEU
SEQRES 31 A 534 ASP ASP ILE VAL GLY ASP HIS ASN VAL ILE CYS PRO LEU
SEQRES 32 A 534 MET HIS PHE VAL ASN LYS TYR THR LYS PHE GLY ASN GLY
SEQRES 33 A 534 THR TYR LEU TYR PHE PHE ASN HIS ARG ALA SER ASN LEU
SEQRES 34 A 534 VAL TRP PRO GLU TRP MET GLY VAL ILE HIS GLY TYR GLU
SEQRES 35 A 534 ILE GLU PHE VAL PHE GLY LEU PRO LEU VAL LYS GLU LEU
SEQRES 36 A 534 ASN TYR THR ALA GLU GLU GLU ALA LEU SER ARG ARG ILE
SEQRES 37 A 534 MET HIS TYR TRP ALA THR PHE ALA LYS THR GLY ASN PRO
SEQRES 38 A 534 ASN GLU PRO HIS SER GLN GLU SER LYS TRP PRO LEU PHE
SEQRES 39 A 534 THR THR LYS GLU GLN LYS PHE ILE ASP LEU ASN THR GLU
SEQRES 40 A 534 PRO MET LYS VAL HIS GLN ARG LEU ARG VAL GLN MET CYS
SEQRES 41 A 534 VAL PHE TRP ASN GLN PHE LEU PRO LYS LEU LEU ASN ALA
SEQRES 42 A 534 THR
HET NAG A 601 14
HET NAG A 602 14
HET NAG A 603 14
HET NAG A 604 14
HET HTB A 605 33
HETNAM NAG N-ACETYL-D-GLUCOSAMINE
HETNAM HTB N-(1-BENZOFURAN-2-YLMETHYL)-N'-(1,2,3,4-
HETNAM 2 HTB TETRAHYDROACRIDIN-9-YL)HEPTANE-1,7-DIAMINE
FORMUL 2 NAG 4(C8 H15 N O6)
FORMUL 5 HTB C29 H35 N3 O
FORMUL 6 HOH *95(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 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 VAL A 277 1 8
HELIX 13 AB4 GLU A 278 LEU A 282 5 5
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 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 ASN A 9 0
SHEET 2 AA1 3 LYS A 14 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 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 SER A 145 -1 O SER A 145 N ASN A 98
SHEET 5 AA211 THR A 109 ILE A 115 1 N MET A 112 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 LEU A 224
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 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
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
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 2.06
LINK ND2 ASN A 59 C1 NAG A 601 1555 1555 1.45
LINK ND2 ASN A 416 C1 NAG A 602 1555 1555 1.46
LINK ND2 ASN A 457 C1 NAG A 604 1555 1555 1.47
LINK O4 NAG A 602 C1 NAG A 603 1555 1555 1.47
CISPEP 1 SER A 103 PRO A 104 0 19.47
CISPEP 2 PHE A 284 ASP A 285 0 1.48
SITE 1 AC1 13 TRP A 84 GLY A 118 GLY A 119 TYR A 121
SITE 2 AC1 13 GLU A 199 SER A 200 TRP A 233 PHE A 290
SITE 3 AC1 13 PHE A 330 VAL A 395 ASN A 399 TRP A 432
SITE 4 AC1 13 HIS A 440
SITE 1 AC2 2 ASN A 59 SER A 61
SITE 1 AC3 4 ASN A 416 HOH A 708 HOH A 772 HOH A 788
SITE 1 AC4 1 ASN A 457
CRYST1 112.220 112.220 138.720 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 0.008911 0.005145 0.000000 0.00000
SCALE2 0.000000 0.010290 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007209 0.00000
TER 4264 THR A 535
MASTER 394 0 5 25 16 0 7 6 4447 1 98 42
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