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HEADER HYDROLASE 15-NOV-17 6EZH
TITLE TORPEDO CALIFORNICA ACHE IN COMPLEX WITH INDOLIC MULTI-TARGET DIRECTED
TITLE 2 LIGAND
CAVEAT 6EZH NAG A 601 HAS WRONG CHIRALITY AT ATOM C1
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ACETYLCHOLINESTERASE;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: ACHE;
COMPND 5 EC: 3.1.1.7
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: TETRONARCE CALIFORNICA;
SOURCE 3 ORGANISM_COMMON: PACIFIC ELECTRIC RAY;
SOURCE 4 ORGANISM_TAXID: 7787
KEYWDS ACETYLCHOLINESTERASE, MULTI-TARGET INHIBITOR, ALZHEIMER DESEASE,
KEYWDS 2 HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR G.SANTONI,J.LALUT,D.KARILA,C.LECOUTEY,A.DAVIS,F.NACHON,I.SILLMAN,
AUTHOR 2 J.SUSSMAN,M.WEIK,T.MAURICE,P.DALLEMAGNE,C.ROCHAIS
REVDAT 1 21-NOV-18 6EZH 0
JRNL AUTH J.LALUT,G.SANTONI,D.KARILA,C.LECOUTEY,A.DAVIS,F.NACHON,
JRNL AUTH 2 I.SILLMAN,J.SUSSMAN,M.WEIK,T.MAURICE,P.DALLEMAGNE,C.ROCHAIS
JRNL TITL NOVEL MULTITARGET-DIRECTED LIGANDS TARGETING
JRNL TITL 2 ACETYLCHOLINESTERASE AND SIGMA1 RECEPTORS AS LEAD COMPOUNDS
JRNL TITL 3 FOR TREATMENT OF ALZHEIMER'S DISEASE: SYNTHESIS, EVALUATION,
JRNL TITL 4 AND STRUCTURAL CHARACTERIZATION OF THEIR COMPLEXES WITH
JRNL TITL 5 ACETYLCHOLINESTERASE
JRNL REF EUR.J.MED.CHEM. 2018
JRNL REFN ISSN 0223-5234
JRNL DOI 10.1016/J.EJMECH.2018.10.064
REMARK 2
REMARK 2 RESOLUTION. 2.60 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0107
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.60
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 46.09
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 3 NUMBER OF REFLECTIONS : 44557
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) : 0.223
REMARK 3 R VALUE (WORKING SET) : 0.222
REMARK 3 FREE R VALUE : 0.273
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 3.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1379
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) : 2.60
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.67
REMARK 3 REFLECTION IN BIN (WORKING SET) : 3229
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.85
REMARK 3 BIN R VALUE (WORKING SET) : 0.2940
REMARK 3 BIN FREE R VALUE SET COUNT : 100
REMARK 3 BIN FREE R VALUE : 0.3630
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 8488
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 114
REMARK 3 SOLVENT ATOMS : 550
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 13.11
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -1.61000
REMARK 3 B22 (A**2) : 5.28000
REMARK 3 B33 (A**2) : -3.67000
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 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.632
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.326
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): NULL
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): NULL
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.934
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.901
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 8876 ; 0.009 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 8115 ; 0.000 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 12059 ; 1.271 ; 1.957
REMARK 3 BOND ANGLES OTHERS (DEGREES): 18693 ; 3.976 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1064 ; 6.204 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 423 ;34.942 ;23.995
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1415 ;16.545 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 49 ;17.366 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1257 ; 0.085 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 10081 ; 0.007 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 2148 ; 0.008 ; 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): 4259 ; 3.126 ; 1.267
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 4258 ; 3.119 ; 1.267
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 5322 ; 4.162 ; 1.881
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 5323 ; 4.165 ; 1.882
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 4617 ; 4.779 ; 1.402
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 4554 ; 4.754 ; 1.382
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 6650 ; 5.843 ; 1.984
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 10880 ; 6.030 ;10.502
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 10602 ; 5.923 ;10.211
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 : NULL
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 6EZH COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 15-NOV-17.
REMARK 100 THE DEPOSITION ID IS D_1200006866.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 28-JUL-13
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID14-4
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.939
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 45936
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.600
REMARK 200 RESOLUTION RANGE LOW (A) : 46.090
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 200 DATA REDUNDANCY : 4.490
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 8.4300
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) : 2.67
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
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: NULL
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: 1EA5
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 59.38
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.03
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 36% PEG 200 150MM MES PH 5.6, VAPOR
REMARK 280 DIFFUSION, HANGING DROP, TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 X+1/2,-Y+1/2,-Z
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 -1.000000 0.000000 0.000000 45.72000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 75.37500
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 53.37000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 75.37500
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 45.72000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 53.37000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2630 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 38920 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 1.0 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 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 B 1
REMARK 465 ASP B 2
REMARK 465 HIS B 3
REMARK 465 ALA B 536
REMARK 465 CYS B 537
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 HOH A 765 O HOH A 838 1.88
REMARK 500 O VAL B 293 O HOH B 701 1.90
REMARK 500 OD2 ASP A 381 O HOH A 701 1.90
REMARK 500 O HOH B 835 O HOH B 919 1.94
REMARK 500 O GLU A 489 O HOH A 702 1.96
REMARK 500 O HOH A 743 O HOH A 955 1.96
REMARK 500 O HOH A 928 O HOH A 966 1.98
REMARK 500 O HOH A 833 O HOH A 867 1.98
REMARK 500 NZ LYS B 14 O HOH B 702 2.02
REMARK 500 NH1 ARG A 88 O HOH A 703 2.02
REMARK 500 O ASN B 416 O HOH B 703 2.03
REMARK 500 OD1 ASP B 393 O HOH B 704 2.03
REMARK 500 OH TYR A 472 O HOH A 704 2.04
REMARK 500 O ALA A 477 O HOH A 705 2.05
REMARK 500 NH2 ARG B 221 O HOH B 705 2.05
REMARK 500 O HOH A 921 O HOH A 951 2.05
REMARK 500 OG1 THR A 193 O HOH A 706 2.06
REMARK 500 O HOH B 892 O HOH B 947 2.06
REMARK 500 O ASN A 85 O HOH A 707 2.07
REMARK 500 O HOH A 747 O HOH A 969 2.09
REMARK 500 O HOH A 805 O HOH A 939 2.09
REMARK 500 NZ LYS B 52 O HOH B 706 2.10
REMARK 500 O HOH A 868 O HOH A 890 2.11
REMARK 500 O HOH B 793 O HOH B 822 2.11
REMARK 500 O MET A 83 O HOH A 708 2.13
REMARK 500 NZ LYS A 52 O HOH A 709 2.13
REMARK 500 O HOH A 894 O HOH A 945 2.14
REMARK 500 O HOH A 857 O HOH A 935 2.14
REMARK 500 OD1 ASN B 42 O HOH B 707 2.15
REMARK 500 ND2 ASN A 533 O HOH A 710 2.15
REMARK 500 O HOH B 915 O HOH B 964 2.15
REMARK 500 O HOH B 786 O HOH B 955 2.15
REMARK 500 O HOH B 751 O HOH B 893 2.15
REMARK 500 O HOH B 749 O HOH B 914 2.15
REMARK 500 OG SER B 12 O HOH B 708 2.16
REMARK 500 O HOH B 896 O HOH B 912 2.16
REMARK 500 NZ LYS B 478 O HOH B 709 2.17
REMARK 500 ND2 ASN A 416 C2 NAG A 602 2.17
REMARK 500 O HOH B 716 O HOH B 920 2.18
REMARK 500 O HOH B 751 O HOH B 951 2.19
REMARK 500 O HOH A 940 O HOH A 965 2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 SER A 24 18.49 58.51
REMARK 500 SER A 25 -157.06 -136.76
REMARK 500 PHE A 45 -8.67 77.04
REMARK 500 ALA A 60 42.76 -105.77
REMARK 500 SER A 200 -115.69 53.21
REMARK 500 GLU A 299 -64.75 -120.41
REMARK 500 THR A 317 -147.68 -159.02
REMARK 500 ASP A 326 60.84 -114.83
REMARK 500 VAL A 360 64.73 -115.20
REMARK 500 ASP A 380 38.26 -165.29
REMARK 500 VAL A 400 -68.58 -123.62
REMARK 500 SER A 487 117.74 76.32
REMARK 500 GLN A 488 -18.23 69.52
REMARK 500 LYS A 498 -73.62 -65.66
REMARK 500 ARG A 517 48.76 33.01
REMARK 500 LEU B 23 61.01 38.26
REMARK 500 SER B 25 -158.31 -144.76
REMARK 500 PHE B 45 -12.66 71.31
REMARK 500 ALA B 60 54.89 -96.29
REMARK 500 PRO B 64 -168.15 -75.99
REMARK 500 SER B 200 -115.63 56.78
REMARK 500 GLU B 299 -57.49 -131.48
REMARK 500 THR B 317 -154.24 -145.82
REMARK 500 ASP B 380 33.42 -153.80
REMARK 500 VAL B 400 -69.97 -120.73
REMARK 500 HIS B 440 122.57 -36.80
REMARK 500 HIS B 486 50.41 35.78
REMARK 500 ASN B 506 -166.08 -163.77
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 GLN A 488 GLU A 489 128.80
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 C6H A 603
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue C6H B 603
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
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: AC4
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: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG B 601 bound
REMARK 800 to ASN B 59
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG B 602 bound
REMARK 800 to ASN B 416
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1EA5 RELATED DB: PDB
REMARK 900 RELATED ID: 2W75 RELATED DB: PDB
REMARK 900 RELATED ID: 1EVE RELATED DB: PDB
REMARK 900 RELATED ID: 6EZG RELATED DB: PDB
DBREF 6EZH A 1 537 UNP P04058 ACES_TETCF 22 558
DBREF 6EZH B 1 537 UNP P04058 ACES_TETCF 22 558
SEQRES 1 A 537 ASP ASP HIS SER GLU LEU LEU VAL ASN THR LYS SER GLY
SEQRES 2 A 537 LYS VAL MET GLY THR ARG VAL PRO VAL LEU SER SER HIS
SEQRES 3 A 537 ILE SER ALA PHE LEU GLY ILE PRO PHE ALA GLU PRO PRO
SEQRES 4 A 537 VAL GLY ASN MET ARG PHE ARG ARG PRO GLU PRO LYS LYS
SEQRES 5 A 537 PRO TRP SER GLY VAL TRP ASN ALA SER THR TYR PRO ASN
SEQRES 6 A 537 ASN CYS GLN GLN TYR VAL ASP GLU GLN PHE PRO GLY PHE
SEQRES 7 A 537 SER GLY SER GLU MET TRP ASN PRO ASN ARG GLU MET SER
SEQRES 8 A 537 GLU ASP CYS LEU TYR LEU ASN ILE TRP VAL PRO SER PRO
SEQRES 9 A 537 ARG PRO LYS SER THR THR VAL MET VAL TRP ILE TYR GLY
SEQRES 10 A 537 GLY GLY PHE TYR SER GLY SER SER THR LEU ASP VAL TYR
SEQRES 11 A 537 ASN GLY LYS TYR LEU ALA TYR THR GLU GLU VAL VAL LEU
SEQRES 12 A 537 VAL SER LEU SER TYR ARG VAL GLY ALA PHE GLY PHE LEU
SEQRES 13 A 537 ALA LEU HIS GLY SER GLN GLU ALA PRO GLY ASN VAL GLY
SEQRES 14 A 537 LEU LEU ASP GLN ARG MET ALA LEU GLN TRP VAL HIS ASP
SEQRES 15 A 537 ASN ILE GLN PHE PHE GLY GLY ASP PRO LYS THR VAL THR
SEQRES 16 A 537 ILE PHE GLY GLU SER ALA GLY GLY ALA SER VAL GLY MET
SEQRES 17 A 537 HIS ILE LEU SER PRO GLY SER ARG ASP LEU PHE ARG ARG
SEQRES 18 A 537 ALA ILE LEU GLN SER GLY SER PRO ASN CYS PRO TRP ALA
SEQRES 19 A 537 SER VAL SER VAL ALA GLU GLY ARG ARG ARG ALA VAL GLU
SEQRES 20 A 537 LEU GLY ARG ASN LEU ASN CYS ASN LEU ASN SER ASP GLU
SEQRES 21 A 537 GLU LEU ILE HIS CYS LEU ARG GLU LYS LYS PRO GLN GLU
SEQRES 22 A 537 LEU ILE ASP VAL GLU TRP ASN VAL LEU PRO PHE ASP SER
SEQRES 23 A 537 ILE PHE ARG PHE SER PHE VAL PRO VAL ILE ASP GLY GLU
SEQRES 24 A 537 PHE PHE PRO THR SER LEU GLU SER MET LEU ASN SER GLY
SEQRES 25 A 537 ASN PHE LYS LYS THR GLN ILE LEU LEU GLY VAL ASN LYS
SEQRES 26 A 537 ASP GLU GLY SER PHE PHE LEU LEU TYR GLY ALA PRO GLY
SEQRES 27 A 537 PHE SER LYS ASP SER GLU SER LYS ILE SER ARG GLU ASP
SEQRES 28 A 537 PHE MET SER GLY VAL LYS LEU SER VAL PRO HIS ALA ASN
SEQRES 29 A 537 ASP LEU GLY LEU ASP ALA VAL THR LEU GLN TYR THR ASP
SEQRES 30 A 537 TRP MET ASP ASP ASN ASN GLY ILE LYS ASN ARG ASP GLY
SEQRES 31 A 537 LEU ASP ASP ILE VAL GLY ASP HIS ASN VAL ILE CYS PRO
SEQRES 32 A 537 LEU MET HIS PHE VAL ASN LYS TYR THR LYS PHE GLY ASN
SEQRES 33 A 537 GLY THR TYR LEU TYR PHE PHE ASN HIS ARG ALA SER ASN
SEQRES 34 A 537 LEU VAL TRP PRO GLU TRP MET GLY VAL ILE HIS GLY TYR
SEQRES 35 A 537 GLU ILE GLU PHE VAL PHE GLY LEU PRO LEU VAL LYS GLU
SEQRES 36 A 537 LEU ASN TYR THR ALA GLU GLU GLU ALA LEU SER ARG ARG
SEQRES 37 A 537 ILE MET HIS TYR TRP ALA THR PHE ALA LYS THR GLY ASN
SEQRES 38 A 537 PRO ASN GLU PRO HIS SER GLN GLU SER LYS TRP PRO LEU
SEQRES 39 A 537 PHE THR THR LYS GLU GLN LYS PHE ILE ASP LEU ASN THR
SEQRES 40 A 537 GLU PRO MET LYS VAL HIS GLN ARG LEU ARG VAL GLN MET
SEQRES 41 A 537 CYS VAL PHE TRP ASN GLN PHE LEU PRO LYS LEU LEU ASN
SEQRES 42 A 537 ALA THR ALA CYS
SEQRES 1 B 537 ASP ASP HIS SER GLU LEU LEU VAL ASN THR LYS SER GLY
SEQRES 2 B 537 LYS VAL MET GLY THR ARG VAL PRO VAL LEU SER SER HIS
SEQRES 3 B 537 ILE SER ALA PHE LEU GLY ILE PRO PHE ALA GLU PRO PRO
SEQRES 4 B 537 VAL GLY ASN MET ARG PHE ARG ARG PRO GLU PRO LYS LYS
SEQRES 5 B 537 PRO TRP SER GLY VAL TRP ASN ALA SER THR TYR PRO ASN
SEQRES 6 B 537 ASN CYS GLN GLN TYR VAL ASP GLU GLN PHE PRO GLY PHE
SEQRES 7 B 537 SER GLY SER GLU MET TRP ASN PRO ASN ARG GLU MET SER
SEQRES 8 B 537 GLU ASP CYS LEU TYR LEU ASN ILE TRP VAL PRO SER PRO
SEQRES 9 B 537 ARG PRO LYS SER THR THR VAL MET VAL TRP ILE TYR GLY
SEQRES 10 B 537 GLY GLY PHE TYR SER GLY SER SER THR LEU ASP VAL TYR
SEQRES 11 B 537 ASN GLY LYS TYR LEU ALA TYR THR GLU GLU VAL VAL LEU
SEQRES 12 B 537 VAL SER LEU SER TYR ARG VAL GLY ALA PHE GLY PHE LEU
SEQRES 13 B 537 ALA LEU HIS GLY SER GLN GLU ALA PRO GLY ASN VAL GLY
SEQRES 14 B 537 LEU LEU ASP GLN ARG MET ALA LEU GLN TRP VAL HIS ASP
SEQRES 15 B 537 ASN ILE GLN PHE PHE GLY GLY ASP PRO LYS THR VAL THR
SEQRES 16 B 537 ILE PHE GLY GLU SER ALA GLY GLY ALA SER VAL GLY MET
SEQRES 17 B 537 HIS ILE LEU SER PRO GLY SER ARG ASP LEU PHE ARG ARG
SEQRES 18 B 537 ALA ILE LEU GLN SER GLY SER PRO ASN CYS PRO TRP ALA
SEQRES 19 B 537 SER VAL SER VAL ALA GLU GLY ARG ARG ARG ALA VAL GLU
SEQRES 20 B 537 LEU GLY ARG ASN LEU ASN CYS ASN LEU ASN SER ASP GLU
SEQRES 21 B 537 GLU LEU ILE HIS CYS LEU ARG GLU LYS LYS PRO GLN GLU
SEQRES 22 B 537 LEU ILE ASP VAL GLU TRP ASN VAL LEU PRO PHE ASP SER
SEQRES 23 B 537 ILE PHE ARG PHE SER PHE VAL PRO VAL ILE ASP GLY GLU
SEQRES 24 B 537 PHE PHE PRO THR SER LEU GLU SER MET LEU ASN SER GLY
SEQRES 25 B 537 ASN PHE LYS LYS THR GLN ILE LEU LEU GLY VAL ASN LYS
SEQRES 26 B 537 ASP GLU GLY SER PHE PHE LEU LEU TYR GLY ALA PRO GLY
SEQRES 27 B 537 PHE SER LYS ASP SER GLU SER LYS ILE SER ARG GLU ASP
SEQRES 28 B 537 PHE MET SER GLY VAL LYS LEU SER VAL PRO HIS ALA ASN
SEQRES 29 B 537 ASP LEU GLY LEU ASP ALA VAL THR LEU GLN TYR THR ASP
SEQRES 30 B 537 TRP MET ASP ASP ASN ASN GLY ILE LYS ASN ARG ASP GLY
SEQRES 31 B 537 LEU ASP ASP ILE VAL GLY ASP HIS ASN VAL ILE CYS PRO
SEQRES 32 B 537 LEU MET HIS PHE VAL ASN LYS TYR THR LYS PHE GLY ASN
SEQRES 33 B 537 GLY THR TYR LEU TYR PHE PHE ASN HIS ARG ALA SER ASN
SEQRES 34 B 537 LEU VAL TRP PRO GLU TRP MET GLY VAL ILE HIS GLY TYR
SEQRES 35 B 537 GLU ILE GLU PHE VAL PHE GLY LEU PRO LEU VAL LYS GLU
SEQRES 36 B 537 LEU ASN TYR THR ALA GLU GLU GLU ALA LEU SER ARG ARG
SEQRES 37 B 537 ILE MET HIS TYR TRP ALA THR PHE ALA LYS THR GLY ASN
SEQRES 38 B 537 PRO ASN GLU PRO HIS SER GLN GLU SER LYS TRP PRO LEU
SEQRES 39 B 537 PHE THR THR LYS GLU GLN LYS PHE ILE ASP LEU ASN THR
SEQRES 40 B 537 GLU PRO MET LYS VAL HIS GLN ARG LEU ARG VAL GLN MET
SEQRES 41 B 537 CYS VAL PHE TRP ASN GLN PHE LEU PRO LYS LEU LEU ASN
SEQRES 42 B 537 ALA THR ALA CYS
HET NAG A 601 14
HET NAG A 602 14
HET C6H A 603 29
HET NAG B 601 14
HET NAG B 602 14
HET C6H B 603 29
HETNAM NAG N-ACETYL-D-GLUCOSAMINE
HETNAM C6H 1-(7-CHLORANYL-4-METHOXY-1~{H}-INDOL-5-YL)-3-[1-
HETNAM 2 C6H (CYCLOHEXYLMETHYL)PIPERIDIN-4-YL]PROPAN-1-ONE
HETSYN C6H MR28926
FORMUL 3 NAG 4(C8 H15 N O6)
FORMUL 5 C6H 2(C24 H33 CL N2 O2)
FORMUL 9 HOH *550(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 139 1 8
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 PRO A 213 PHE A 219 5 7
HELIX 10 AB1 SER A 237 ASN A 251 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 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
HELIX 26 AC8 VAL B 40 ARG B 44 5 5
HELIX 27 AC9 PHE B 78 MET B 83 1 6
HELIX 28 AD1 LEU B 127 ASN B 131 5 5
HELIX 29 AD2 GLY B 132 GLU B 140 1 9
HELIX 30 AD3 VAL B 150 LEU B 156 1 7
HELIX 31 AD4 ASN B 167 ILE B 184 1 18
HELIX 32 AD5 GLN B 185 PHE B 187 5 3
HELIX 33 AD6 SER B 200 SER B 212 1 13
HELIX 34 AD7 PRO B 213 PHE B 219 5 7
HELIX 35 AD8 VAL B 238 ASN B 251 1 14
HELIX 36 AD9 SER B 258 LYS B 269 1 12
HELIX 37 AE1 LYS B 270 GLU B 278 1 9
HELIX 38 AE2 TRP B 279 LEU B 282 5 4
HELIX 39 AE3 SER B 304 GLY B 312 1 9
HELIX 40 AE4 GLY B 328 ALA B 336 1 9
HELIX 41 AE5 SER B 348 VAL B 360 1 13
HELIX 42 AE6 ASN B 364 THR B 376 1 13
HELIX 43 AE7 ASN B 383 VAL B 400 1 18
HELIX 44 AE8 VAL B 400 LYS B 413 1 14
HELIX 45 AE9 PRO B 433 GLY B 437 5 5
HELIX 46 AF1 GLU B 443 PHE B 448 1 6
HELIX 47 AF2 GLY B 449 ASN B 457 5 9
HELIX 48 AF3 THR B 459 GLY B 480 1 22
HELIX 49 AF4 ARG B 517 GLN B 526 1 10
HELIX 50 AF5 GLN B 526 ALA B 534 1 9
SHEET 1 AA1 3 LEU A 7 THR A 10 0
SHEET 2 AA1 3 GLY A 13 MET A 16 -1 O GLY A 13 N THR A 10
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 ALA A 29 N THR A 18
SHEET 3 AA211 TYR A 96 PRO A 102 -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 111
SHEET 7 AA211 ARG A 221 GLN A 225 1 O GLN A 225 N GLY A 198
SHEET 8 AA211 ILE A 319 ASN A 324 1 O LEU A 320 N ALA A 222
SHEET 9 AA211 THR A 418 PHE A 423 1 O PHE A 423 N VAL A 323
SHEET 10 AA211 LYS A 501 LEU A 505 1 O LEU A 505 N PHE A 422
SHEET 11 AA211 VAL A 512 GLN A 514 -1 O HIS A 513 N PHE A 502
SHEET 1 AA3 2 ASN A 66 CYS A 67 0
SHEET 2 AA3 2 MET A 90 SER A 91 1 O SER A 91 N ASN A 66
SHEET 1 AA4 3 LEU B 7 THR B 10 0
SHEET 2 AA4 3 GLY B 13 MET B 16 -1 O GLY B 13 N THR B 10
SHEET 3 AA4 3 VAL B 57 ASN B 59 1 O TRP B 58 N MET B 16
SHEET 1 AA511 THR B 18 VAL B 22 0
SHEET 2 AA511 SER B 25 PRO B 34 -1 O ALA B 29 N THR B 18
SHEET 3 AA511 TYR B 96 VAL B 101 -1 O VAL B 101 N SER B 28
SHEET 4 AA511 VAL B 142 SER B 145 -1 O SER B 145 N ASN B 98
SHEET 5 AA511 THR B 109 ILE B 115 1 N TRP B 114 O VAL B 144
SHEET 6 AA511 GLY B 189 GLU B 199 1 O ASP B 190 N THR B 109
SHEET 7 AA511 ARG B 221 GLN B 225 1 O ILE B 223 N ILE B 196
SHEET 8 AA511 ILE B 319 ASN B 324 1 O LEU B 320 N ALA B 222
SHEET 9 AA511 THR B 418 PHE B 423 1 O PHE B 423 N VAL B 323
SHEET 10 AA511 LYS B 501 LEU B 505 1 O ILE B 503 N PHE B 422
SHEET 11 AA511 VAL B 512 GLN B 514 -1 O HIS B 513 N PHE B 502
SHEET 1 AA6 2 VAL B 236 SER B 237 0
SHEET 2 AA6 2 VAL B 295 ILE B 296 1 O ILE B 296 N VAL B 236
SSBOND 1 CYS A 67 CYS A 94 1555 1555 2.02
SSBOND 2 CYS A 254 CYS A 265 1555 1555 2.03
SSBOND 3 CYS A 402 CYS A 521 1555 1555 2.03
SSBOND 4 CYS B 67 CYS B 94 1555 1555 2.05
SSBOND 5 CYS B 254 CYS B 265 1555 1555 2.03
SSBOND 6 CYS B 402 CYS B 521 1555 1555 2.05
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 B 59 C1 NAG B 601 1555 1555 1.44
LINK ND2 ASN B 416 C1 NAG B 602 1555 1555 1.45
CISPEP 1 SER A 103 PRO A 104 0 7.63
CISPEP 2 SER A 487 GLN A 488 0 24.03
CISPEP 3 GLU A 489 SER A 490 0 -14.90
CISPEP 4 SER B 103 PRO B 104 0 12.50
SITE 1 AC1 13 TYR A 70 TRP A 84 GLY A 118 TYR A 121
SITE 2 AC1 13 GLU A 199 SER A 286 PHE A 330 PHE A 331
SITE 3 AC1 13 TYR A 334 HIS A 440 GLY A 441 HOH A 918
SITE 4 AC1 13 HOH A 927
SITE 1 AC2 7 TYR B 70 GLY B 118 TYR B 121 GLU B 199
SITE 2 AC2 7 PHE B 288 PHE B 330 HOH B 836
SITE 1 AC3 2 ASN A 59 SER A 61
SITE 1 AC4 4 ASN A 416 HOH A 745 HOH A 778 HOH A 876
SITE 1 AC5 6 ASN B 59 SER B 61 HOH B 793 HOH B 803
SITE 2 AC5 6 HOH B 822 HOH B 848
SITE 1 AC6 5 ASN B 416 HOH B 735 HOH B 799 HOH B 800
SITE 2 AC6 5 HOH B 891
CRYST1 91.440 106.740 150.750 90.00 90.00 90.00 P 21 21 21 8
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 0.010936 0.000000 0.000000 0.00000
SCALE2 0.000000 0.009369 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006633 0.00000
TER 4245 THR A 535
TER 8501 THR B 535
MASTER 398 0 6 50 32 0 12 6 9152 2 130 84
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