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HEADER HYDROLASE 30-OCT-17 6EUE
TITLE RIVASTIGMINE ANALOGUE BOUND TO TC ACHE.
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ACETYLCHOLINESTERASE;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: ACHE;
COMPND 5 EC: 3.1.1.7;
COMPND 6 OTHER_DETAILS: TC ACHE WITH CARBAMYLATED SER200
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: TETRONARCE CALIFORNICA;
SOURCE 3 ORGANISM_COMMON: PACIFIC ELECTRIC RAY;
SOURCE 4 ORGANISM_TAXID: 7787
KEYWDS CHOLINESTERASE, ALZHEIMER DISEASE, ORGANOPHOSPHATE, CARBAMYLATED,
KEYWDS 2 HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR E.DE LA MORA,X.BRAZZOLOTTO,S.N.DIGHE,I.SILMAN,M.WEIK,B.ROSS
REVDAT 1 14-NOV-18 6EUE 0
JRNL AUTH S.N.DIGHE,E.DE LA MORA,S.CHAN,S.KANTHAM,G.MCCOLL,
JRNL AUTH 2 S.K.VELIYAT,J.A.MILES,R.P.MCGEARY,I.SILMAN,M.WEIK,M.P.PARAT,
JRNL AUTH 3 X.BRAZZOLOTTO,B.ROSS
JRNL TITL ANALOGUES OF RIVASTIGMINE AND NAP FOR THE CNS DELIVERY OF
JRNL TITL 2 POLYPHENOLS WITH PUTATIVE ALZHEIMER DISEASE-MODIFYING
JRNL TITL 3 PROPERTIES
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (1.11.1_2575: ???)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 39.60
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 3 NUMBER OF REFLECTIONS : 67375
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.197
REMARK 3 R VALUE (WORKING SET) : 0.196
REMARK 3 FREE R VALUE : 0.225
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.210
REMARK 3 FREE R VALUE TEST SET COUNT : 3508
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 39.5900 - 5.8420 1.00 2746 137 0.1843 0.1928
REMARK 3 2 5.8420 - 4.6393 1.00 2620 154 0.1504 0.1675
REMARK 3 3 4.6393 - 4.0535 1.00 2618 133 0.1375 0.1530
REMARK 3 4 4.0535 - 3.6832 1.00 2607 126 0.1489 0.1766
REMARK 3 5 3.6832 - 3.4194 1.00 2559 156 0.1656 0.1901
REMARK 3 6 3.4194 - 3.2179 1.00 2583 132 0.1813 0.2250
REMARK 3 7 3.2179 - 3.0568 1.00 2546 142 0.1999 0.2615
REMARK 3 8 3.0568 - 2.9237 1.00 2556 154 0.1953 0.2153
REMARK 3 9 2.9237 - 2.8112 1.00 2545 143 0.1849 0.2262
REMARK 3 10 2.8112 - 2.7142 1.00 2563 163 0.1933 0.2432
REMARK 3 11 2.7142 - 2.6294 1.00 2511 154 0.2048 0.2734
REMARK 3 12 2.6294 - 2.5542 1.00 2533 133 0.2115 0.2622
REMARK 3 13 2.5542 - 2.4870 1.00 2541 149 0.2266 0.3000
REMARK 3 14 2.4870 - 2.4263 1.00 2509 179 0.2382 0.2901
REMARK 3 15 2.4263 - 2.3712 1.00 2575 113 0.2377 0.2599
REMARK 3 16 2.3712 - 2.3207 1.00 2497 161 0.2594 0.2753
REMARK 3 17 2.3207 - 2.2743 0.99 2546 128 0.2629 0.2648
REMARK 3 18 2.2743 - 2.2314 0.99 2548 123 0.2728 0.3520
REMARK 3 19 2.2314 - 2.1916 1.00 2533 125 0.2939 0.3299
REMARK 3 20 2.1916 - 2.1544 0.99 2527 119 0.3140 0.3320
REMARK 3 21 2.1544 - 2.1197 0.99 2523 156 0.3143 0.3618
REMARK 3 22 2.1197 - 2.0871 1.00 2512 128 0.3383 0.3384
REMARK 3 23 2.0871 - 2.0564 0.99 2543 149 0.3568 0.3714
REMARK 3 24 2.0564 - 2.0274 0.99 2474 134 0.3802 0.3684
REMARK 3 25 2.0274 - 2.0000 1.00 2552 117 0.3700 0.3700
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.260
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 28.170
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 37.82
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.011 4547
REMARK 3 ANGLE : 1.971 6177
REMARK 3 CHIRALITY : 0.120 645
REMARK 3 PLANARITY : 0.008 803
REMARK 3 DIHEDRAL : 19.094 1696
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 6EUE COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 30-OCT-17.
REMARK 100 THE DEPOSITION ID IS D_1200007036.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 31-OCT-15
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID23-2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS3 S 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 67469
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000
REMARK 200 RESOLUTION RANGE LOW (A) : 39.600
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.900
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 200 DATA REDUNDANCY : 6.400
REMARK 200 R MERGE (I) : 0.07100
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 13.5200
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.07
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.4
REMARK 200 DATA REDUNDANCY IN SHELL : 6.50
REMARK 200 R MERGE FOR SHELL (I) : 0.66000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 1.890
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: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 70.21
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.13
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: MES 100 MM PH 5.5 PEG 200 32%, VAPOR
REMARK 280 DIFFUSION, TEMPERATURE 295K
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 45.71667
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 91.43333
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 91.43333
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 45.71667
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: 5420 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 39310 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 8.0 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 350 BIOMT1 2 -0.500000 -0.866025 0.000000 168.00000
REMARK 350 BIOMT2 2 -0.866025 0.500000 0.000000 96.99485
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 320.01667
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 HIS A 3
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 ASN A 42 CG OD1 ND2
REMARK 470 LYS A 491 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 CE2 PHE A 330 O HOH A 808 1.54
REMARK 500 OE1 GLU A 344 NZ LYS A 346 1.65
REMARK 500 CZ PHE A 330 O HOH A 808 1.93
REMARK 500 O ASN A 457 O HOH A 802 1.94
REMARK 500 OE1 GLU A 327 ND1 HIS A 440 2.03
REMARK 500 O HOH A 1057 O HOH A 1145 2.16
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 GLU A 350 N GLU A 350 CA 0.127
REMARK 500 MET A 379 CA MET A 379 C 0.176
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 MET A 43 N - CA - C ANGL. DEV. = 18.1 DEGREES
REMARK 500 ARG A 88 N - CA - C ANGL. DEV. = 23.0 DEGREES
REMARK 500 ARG A 88 CA - C - O ANGL. DEV. = -13.5 DEGREES
REMARK 500 ARG A 88 CA - C - O ANGL. DEV. = -17.8 DEGREES
REMARK 500 ARG A 88 CA - C - N ANGL. DEV. = 17.5 DEGREES
REMARK 500 GLU A 140 N - CA - C ANGL. DEV. = 16.9 DEGREES
REMARK 500 GLU A 140 CA - C - O ANGL. DEV. = 17.4 DEGREES
REMARK 500 GLU A 140 CA - C - N ANGL. DEV. = -17.6 DEGREES
REMARK 500 LYS A 192 CA - C - O ANGL. DEV. = 16.1 DEGREES
REMARK 500 LYS A 192 CA - C - N ANGL. DEV. = -13.4 DEGREES
REMARK 500 PHE A 330 CA - C - O ANGL. DEV. = 17.7 DEGREES
REMARK 500 PHE A 330 CA - C - O ANGL. DEV. = 15.2 DEGREES
REMARK 500 PHE A 330 CA - C - N ANGL. DEV. = -14.8 DEGREES
REMARK 500 GLU A 350 C - N - CA ANGL. DEV. = -15.3 DEGREES
REMARK 500 GLU A 350 N - CA - C ANGL. DEV. = 16.8 DEGREES
REMARK 500 MET A 379 CA - C - N ANGL. DEV. = -15.8 DEGREES
REMARK 500 HIS A 440 CB - CA - C ANGL. DEV. = 14.9 DEGREES
REMARK 500 LEU A 456 CA - C - N ANGL. DEV. = 14.4 DEGREES
REMARK 500 LEU A 456 O - C - N ANGL. DEV. = -18.5 DEGREES
REMARK 500 ASN A 457 CB - CA - C ANGL. DEV. = 35.1 DEGREES
REMARK 500 ASN A 457 N - CA - C ANGL. DEV. = -22.5 DEGREES
REMARK 500 TYR A 458 C - N - CA ANGL. DEV. = 41.5 DEGREES
REMARK 500 TYR A 458 N - CA - CB ANGL. DEV. = 26.4 DEGREES
REMARK 500 GLU A 489 CB - CA - C ANGL. DEV. = -13.9 DEGREES
REMARK 500 GLU A 489 N - CA - C ANGL. DEV. = 19.3 DEGREES
REMARK 500 GLU A 489 N - CA - C ANGL. DEV. = 23.5 DEGREES
REMARK 500 GLU A 489 CA - C - O ANGL. DEV. = -26.5 DEGREES
REMARK 500 GLU A 489 CA - C - O ANGL. DEV. = -26.2 DEGREES
REMARK 500 GLU A 489 CA - C - N ANGL. DEV. = 25.6 DEGREES
REMARK 500 GLU A 489 CA - C - N ANGL. DEV. = 23.3 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 SER A 25 -157.80 -120.81
REMARK 500 PHE A 45 -10.36 79.27
REMARK 500 ALA A 60 41.63 -106.86
REMARK 500 CYS A 94 10.72 -145.67
REMARK 500 SER A 108 77.70 -159.05
REMARK 500 ASN A 131 106.19 -58.30
REMARK 500 GLU A 140 65.96 32.60
REMARK 500 PHE A 155 10.34 -140.30
REMARK 500 BXT A 200 -122.42 67.01
REMARK 500 GLU A 299 -74.00 -113.94
REMARK 500 ASP A 380 55.61 -142.61
REMARK 500 VAL A 400 -60.07 -129.89
REMARK 500 HIS A 440 110.78 -16.66
REMARK 500 HIS A 440 112.21 -16.72
REMARK 500 ASN A 457 -145.24 96.19
REMARK 500 ASN A 457 38.71 109.65
REMARK 500 TYR A 458 123.64 91.90
REMARK 500 ARG A 515 62.14 61.78
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 ASN A 87 ARG A 88 148.87
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY
REMARK 500
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 500 I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI ANGLE
REMARK 500 GLU A 350 -10.25
REMARK 500 LEU A 456 14.15
REMARK 500 GLU A 489 13.71
REMARK 500
REMARK 500 REMARK: NULL
REMARK 610
REMARK 610 MISSING HETEROATOM
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 610 I=INSERTION CODE):
REMARK 610 M RES C SSEQI
REMARK 610 1PE A 701
REMARK 610 1PE A 702
REMARK 610 1PE A 703
REMARK 610 1PE A 704
REMARK 610 1PE A 705
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 1PE A 701
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 1PE A 702
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 1PE A 703
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 1PE A 704
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 1PE A 705
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG A 706 bound
REMARK 800 to ASN A 59
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG A 707 bound
REMARK 800 to ASN A 416
DBREF 6EUE A 3 535 UNP P04058 ACES_TETCF 24 556
SEQRES 1 A 533 HIS SER GLU LEU LEU VAL ASN THR LYS SER GLY LYS VAL
SEQRES 2 A 533 MET GLY THR ARG VAL PRO VAL LEU SER SER HIS ILE SER
SEQRES 3 A 533 ALA PHE LEU GLY ILE PRO PHE ALA GLU PRO PRO VAL GLY
SEQRES 4 A 533 ASN MET ARG PHE ARG ARG PRO GLU PRO LYS LYS PRO TRP
SEQRES 5 A 533 SER GLY VAL TRP ASN ALA SER THR TYR PRO ASN ASN CYS
SEQRES 6 A 533 GLN GLN TYR VAL ASP GLU GLN PHE PRO GLY PHE SER GLY
SEQRES 7 A 533 SER GLU MET TRP ASN PRO ASN ARG GLU MET SER GLU ASP
SEQRES 8 A 533 CYS LEU TYR LEU ASN ILE TRP VAL PRO SER PRO ARG PRO
SEQRES 9 A 533 LYS SER THR THR VAL MET VAL TRP ILE TYR GLY GLY GLY
SEQRES 10 A 533 PHE TYR SER GLY SER SER THR LEU ASP VAL TYR ASN GLY
SEQRES 11 A 533 LYS TYR LEU ALA TYR THR GLU GLU VAL VAL LEU VAL SER
SEQRES 12 A 533 LEU SER TYR ARG VAL GLY ALA PHE GLY PHE LEU ALA LEU
SEQRES 13 A 533 HIS GLY SER GLN GLU ALA PRO GLY ASN VAL GLY LEU LEU
SEQRES 14 A 533 ASP GLN ARG MET ALA LEU GLN TRP VAL HIS ASP ASN ILE
SEQRES 15 A 533 GLN PHE PHE GLY GLY ASP PRO LYS THR VAL THR ILE PHE
SEQRES 16 A 533 GLY GLU BXT ALA GLY GLY ALA SER VAL GLY MET HIS ILE
SEQRES 17 A 533 LEU SER PRO GLY SER ARG ASP LEU PHE ARG ARG ALA ILE
SEQRES 18 A 533 LEU GLN SER GLY SER PRO ASN CYS PRO TRP ALA SER VAL
SEQRES 19 A 533 SER VAL ALA GLU GLY ARG ARG ARG ALA VAL GLU LEU GLY
SEQRES 20 A 533 ARG ASN LEU ASN CYS ASN LEU ASN SER ASP GLU GLU LEU
SEQRES 21 A 533 ILE HIS CYS LEU ARG GLU LYS LYS PRO GLN GLU LEU ILE
SEQRES 22 A 533 ASP VAL GLU TRP ASN VAL LEU PRO PHE ASP SER ILE PHE
SEQRES 23 A 533 ARG PHE SER PHE VAL PRO VAL ILE ASP GLY GLU PHE PHE
SEQRES 24 A 533 PRO THR SER LEU GLU SER MET LEU ASN SER GLY ASN PHE
SEQRES 25 A 533 LYS LYS THR GLN ILE LEU LEU GLY VAL ASN LYS ASP GLU
SEQRES 26 A 533 GLY SER PHE PHE LEU LEU TYR GLY ALA PRO GLY PHE SER
SEQRES 27 A 533 LYS ASP SER GLU SER LYS ILE SER ARG GLU ASP PHE MET
SEQRES 28 A 533 SER GLY VAL LYS LEU SER VAL PRO HIS ALA ASN ASP LEU
SEQRES 29 A 533 GLY LEU ASP ALA VAL THR LEU GLN TYR THR ASP TRP MET
SEQRES 30 A 533 ASP ASP ASN ASN GLY ILE LYS ASN ARG ASP GLY LEU ASP
SEQRES 31 A 533 ASP ILE VAL GLY ASP HIS ASN VAL ILE CYS PRO LEU MET
SEQRES 32 A 533 HIS PHE VAL ASN LYS TYR THR LYS PHE GLY ASN GLY THR
SEQRES 33 A 533 TYR LEU TYR PHE PHE ASN HIS ARG ALA SER ASN LEU VAL
SEQRES 34 A 533 TRP PRO GLU TRP MET GLY VAL ILE HIS GLY TYR GLU ILE
SEQRES 35 A 533 GLU PHE VAL PHE GLY LEU PRO LEU VAL LYS GLU LEU ASN
SEQRES 36 A 533 TYR THR ALA GLU GLU GLU ALA LEU SER ARG ARG ILE MET
SEQRES 37 A 533 HIS TYR TRP ALA THR PHE ALA LYS THR GLY ASN PRO ASN
SEQRES 38 A 533 GLU PRO HIS SER GLN GLU SER LYS TRP PRO LEU PHE THR
SEQRES 39 A 533 THR LYS GLU GLN LYS PHE ILE ASP LEU ASN THR GLU PRO
SEQRES 40 A 533 MET LYS VAL HIS GLN ARG LEU ARG VAL GLN MET CYS VAL
SEQRES 41 A 533 PHE TRP ASN GLN PHE LEU PRO LYS LEU LEU ASN ALA THR
MODRES 6EUE BXT A 200 SER MODIFIED RESIDUE
HET BXT A 200 12
HET 1PE A 701 14
HET 1PE A 702 10
HET 1PE A 703 7
HET 1PE A 704 7
HET 1PE A 705 7
HET NAG A 706 14
HET NAG A 707 14
HETNAM BXT (2~{S})-2-AZANYL-3-[ETHYL(METHYL)CARBAMOYL]OXY-
HETNAM 2 BXT PROPANOIC ACID
HETNAM 1PE PENTAETHYLENE GLYCOL
HETNAM NAG N-ACETYL-D-GLUCOSAMINE
HETSYN 1PE PEG400
FORMUL 1 BXT C7 H14 N2 O4
FORMUL 2 1PE 5(C10 H22 O6)
FORMUL 7 NAG 2(C8 H15 N O6)
FORMUL 9 HOH *389(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 BXT 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 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
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 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 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 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 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
SSBOND 1 CYS A 67 CYS A 94 1555 1555 2.05
SSBOND 2 CYS A 254 CYS A 265 1555 1555 2.04
SSBOND 3 CYS A 402 CYS A 521 1555 1555 2.05
LINK ND2 ASN A 59 C1 NAG A 706 1555 1555 1.46
LINK C GLU A 199 N BXT A 200 1555 1555 1.33
LINK C BXT A 200 N ALA A 201 1555 1555 1.33
LINK ND2 ASN A 416 C1 NAG A 707 1555 1555 1.45
CISPEP 1 SER A 103 PRO A 104 0 3.08
SITE 1 AC1 11 TRP A 84 GLY A 117 GLY A 118 GLU A 199
SITE 2 AC1 11 BXT A 200 PHE A 330 HIS A 440 HOH A 801
SITE 3 AC1 11 HOH A 808 HOH A 817 HOH A 868
SITE 1 AC2 5 TYR A 121 PHE A 330 HOH A 808 HOH A1102
SITE 2 AC2 5 HOH A1124
SITE 1 AC3 2 ARG A 250 ASN A 253
SITE 1 AC4 3 ILE A 296 SER A 304 HOH A1009
SITE 1 AC5 4 GLN A 374 THR A 376 ASP A 377 HOH A1035
SITE 1 AC6 2 ASN A 59 SER A 61
SITE 1 AC7 2 ASN A 416 HOH A 811
CRYST1 112.000 112.000 137.150 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 0.008929 0.005155 0.000000 0.00000
SCALE2 0.000000 0.010310 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007291 0.00000
TER 4337 THR A 535
MASTER 431 0 8 25 14 0 10 6 4700 1 95 41
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