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HEADER HYDROLASE 07-JUN-14 4TPK
TITLE HUMAN BUTYRYLCHOLINESTERASE IN COMPLEX WITH N-((1-(2,3-DIHYDRO-1H-
TITLE 2 INDEN-2-YL)PIPERIDIN-3-YL)METHYL)-N-(2-METHOXYETHYL)-2-NAPHTHAMIDE
CAVEAT 4TPK NAG A 608 HAS WRONG CHIRALITY AT C1 NAG A 607 HAS WRONG
CAVEAT 2 4TPK CHIRALITY AT C1 NAG B 610 HAS WRONG CHIRALITY AT C1
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CHOLINESTERASE;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: ACYLCHOLINE ACYLHYDROLASE,BUTYRYLCHOLINE ESTERASE,CHOLINE
COMPND 5 ESTERASE II,PSEUDOCHOLINESTERASE;
COMPND 6 EC: 3.1.1.8;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: BCHE, CHE1;
SOURCE 6 EXPRESSION_SYSTEM: CRICETULUS GRISEUS;
SOURCE 7 EXPRESSION_SYSTEM_COMMON: CHINESE HAMSTER;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 10029
KEYWDS BUTYRYLCHOLINESTERASE INHIBITION, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR N.COQUELLE,B.BRUS,J.P.COLLETIER,S.GOBEC
REVDAT 1 22-OCT-14 4TPK 0
JRNL AUTH B.BRUS,U.KOSAK,S.TURK,A.PISLAR,N.COQUELLE,J.KOS,J.STOJAN,
JRNL AUTH 2 J.P.COLLETIER,S.GOBEC
JRNL TITL DISCOVERY, BIOLOGICAL EVALUATION, AND CRYSTAL STRUCTURE OF A
JRNL TITL 2 NOVEL NANOMOLAR SELECTIVE BUTYRYLCHOLINESTERASE INHIBITOR.
JRNL REF J.MED.CHEM. V. 57 8167 2014
JRNL REFN ISSN 0022-2623
JRNL PMID 25226236
JRNL DOI 10.1021/JM501195E
REMARK 2
REMARK 2 RESOLUTION. 2.70 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.8.4_1496)
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 : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.70
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 46.20
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.360
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 3 NUMBER OF REFLECTIONS : 40022
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.186
REMARK 3 R VALUE (WORKING SET) : 0.184
REMARK 3 FREE R VALUE : 0.239
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 3.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1202
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 46.2025 - 5.6133 0.99 4538 140 0.1924 0.2347
REMARK 3 2 5.6133 - 4.4566 1.00 4356 133 0.1560 0.1871
REMARK 3 3 4.4566 - 3.8936 1.00 4346 136 0.1490 0.2021
REMARK 3 4 3.8936 - 3.5377 1.00 4305 136 0.1747 0.2366
REMARK 3 5 3.5377 - 3.2842 1.00 4279 132 0.1990 0.2548
REMARK 3 6 3.2842 - 3.0907 1.00 4233 135 0.2189 0.3258
REMARK 3 7 3.0907 - 2.9359 1.00 4278 126 0.2226 0.3001
REMARK 3 8 2.9359 - 2.8081 1.00 4257 133 0.2354 0.3050
REMARK 3 9 2.8081 - 2.7000 1.00 4228 131 0.2319 0.3154
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
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) : 0.370
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 25.380
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
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 : 0.007 9079
REMARK 3 ANGLE : 1.021 12288
REMARK 3 CHIRALITY : 0.038 1328
REMARK 3 PLANARITY : 0.005 1546
REMARK 3 DIHEDRAL : 14.508 3344
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 4TPK COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 10-JUN-14.
REMARK 100 THE DEPOSITION ID IS D_1000201991.
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 : 7.4
REMARK 200 NUMBER OF CRYSTALS USED : NULL
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) : 0.873
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 : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 40037
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.700
REMARK 200 RESOLUTION RANGE LOW (A) : 46.200
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 5.200
REMARK 200 R MERGE (I) : 0.08829
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 13.6200
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) : 2.80
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.9
REMARK 200 DATA REDUNDANCY IN SHELL : 5.20
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 2.390
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: 1POM
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 47.79
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.36
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2M AMMONIUM ACETATE, 24% PEG 3350,
REMARK 280 10 MM TRIS PH 7.4
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 38.30000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 115.82500
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 40.10000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 115.82500
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 38.30000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 40.10000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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 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
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 MET A -27
REMARK 465 HIS A -26
REMARK 465 SER A -25
REMARK 465 LYS A -24
REMARK 465 VAL A -23
REMARK 465 THR A -22
REMARK 465 ILE A -21
REMARK 465 ILE A -20
REMARK 465 CYS A -19
REMARK 465 ILE A -18
REMARK 465 ARG A -17
REMARK 465 PHE A -16
REMARK 465 LEU A -15
REMARK 465 PHE A -14
REMARK 465 TRP A -13
REMARK 465 PHE A -12
REMARK 465 LEU A -11
REMARK 465 LEU A -10
REMARK 465 LEU A -9
REMARK 465 CYS A -8
REMARK 465 MET A -7
REMARK 465 LEU A -6
REMARK 465 ILE A -5
REMARK 465 GLY A -4
REMARK 465 LYS A -3
REMARK 465 SER A -2
REMARK 465 HIS A -1
REMARK 465 THR A 0
REMARK 465 GLU A 1
REMARK 465 ASP A 2
REMARK 465 GLU A 531
REMARK 465 MET A 532
REMARK 465 THR A 533
REMARK 465 GLY A 534
REMARK 465 ASN A 535
REMARK 465 ILE A 536
REMARK 465 ASP A 537
REMARK 465 GLU A 538
REMARK 465 ALA A 539
REMARK 465 GLU A 540
REMARK 465 TRP A 541
REMARK 465 GLU A 542
REMARK 465 TRP A 543
REMARK 465 LYS A 544
REMARK 465 ALA A 545
REMARK 465 GLY A 546
REMARK 465 PHE A 547
REMARK 465 HIS A 548
REMARK 465 ARG A 549
REMARK 465 TRP A 550
REMARK 465 ASN A 551
REMARK 465 ASN A 552
REMARK 465 TYR A 553
REMARK 465 MET A 554
REMARK 465 MET A 555
REMARK 465 ASP A 556
REMARK 465 TRP A 557
REMARK 465 LYS A 558
REMARK 465 ASN A 559
REMARK 465 GLN A 560
REMARK 465 PHE A 561
REMARK 465 ASN A 562
REMARK 465 ASP A 563
REMARK 465 TYR A 564
REMARK 465 THR A 565
REMARK 465 SER A 566
REMARK 465 LYS A 567
REMARK 465 LYS A 568
REMARK 465 GLU A 569
REMARK 465 SER A 570
REMARK 465 CYS A 571
REMARK 465 VAL A 572
REMARK 465 GLY A 573
REMARK 465 LEU A 574
REMARK 465 MET B -27
REMARK 465 HIS B -26
REMARK 465 SER B -25
REMARK 465 LYS B -24
REMARK 465 VAL B -23
REMARK 465 THR B -22
REMARK 465 ILE B -21
REMARK 465 ILE B -20
REMARK 465 CYS B -19
REMARK 465 ILE B -18
REMARK 465 ARG B -17
REMARK 465 PHE B -16
REMARK 465 LEU B -15
REMARK 465 PHE B -14
REMARK 465 TRP B -13
REMARK 465 PHE B -12
REMARK 465 LEU B -11
REMARK 465 LEU B -10
REMARK 465 LEU B -9
REMARK 465 CYS B -8
REMARK 465 MET B -7
REMARK 465 LEU B -6
REMARK 465 ILE B -5
REMARK 465 GLY B -4
REMARK 465 LYS B -3
REMARK 465 SER B -2
REMARK 465 HIS B -1
REMARK 465 THR B 0
REMARK 465 GLU B 1
REMARK 465 ASP B 2
REMARK 465 ASP B 3
REMARK 465 GLN B 484
REMARK 465 ASN B 485
REMARK 465 GLU B 531
REMARK 465 MET B 532
REMARK 465 THR B 533
REMARK 465 GLY B 534
REMARK 465 ASN B 535
REMARK 465 ILE B 536
REMARK 465 ASP B 537
REMARK 465 GLU B 538
REMARK 465 ALA B 539
REMARK 465 GLU B 540
REMARK 465 TRP B 541
REMARK 465 GLU B 542
REMARK 465 TRP B 543
REMARK 465 LYS B 544
REMARK 465 ALA B 545
REMARK 465 GLY B 546
REMARK 465 PHE B 547
REMARK 465 HIS B 548
REMARK 465 ARG B 549
REMARK 465 TRP B 550
REMARK 465 ASN B 551
REMARK 465 ASN B 552
REMARK 465 TYR B 553
REMARK 465 MET B 554
REMARK 465 MET B 555
REMARK 465 ASP B 556
REMARK 465 TRP B 557
REMARK 465 LYS B 558
REMARK 465 ASN B 559
REMARK 465 GLN B 560
REMARK 465 PHE B 561
REMARK 465 ASN B 562
REMARK 465 ASP B 563
REMARK 465 TYR B 564
REMARK 465 THR B 565
REMARK 465 SER B 566
REMARK 465 LYS B 567
REMARK 465 LYS B 568
REMARK 465 GLU B 569
REMARK 465 SER B 570
REMARK 465 CYS B 571
REMARK 465 VAL B 572
REMARK 465 GLY B 573
REMARK 465 LEU B 574
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 GLU A 255 CG CD OE1 OE2
REMARK 470 TYR A 282 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 GLU A 506 CG CD OE1 OE2
REMARK 470 LEU A 530 CA C O CB CG CD1 CD2
REMARK 470 ILE B 4 CG1 CG2 CD1
REMARK 470 LYS B 51 CG CD CE NZ
REMARK 470 SER B 53 OG
REMARK 470 TYR B 282 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 ASN B 486 CG OD1 ND2
REMARK 470 SER B 507 CB OG
REMARK 470 LEU B 530 CA C O CB CG CD1 CD2
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 ILE B 4 O
REMARK 480 SER B 53 CB
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 ND2 ASN A 341 C1 NAG A 608 1.41
REMARK 500 O4 NAG A 608 C1 NAG A 609 1.41
REMARK 500 O6 NAG A 608 C1 FUC A 610 1.46
REMARK 500 ND2 ASN B 481 C1 NAG B 610 1.46
REMARK 500 ND2 ASN B 17 O5 NAG B 601 1.61
REMARK 500 ND2 ASN A 341 O5 NAG A 608 1.64
REMARK 500 ND2 ASN B 256 O5 NAG B 608 1.66
REMARK 500 O4 NAG A 604 O5 NAG A 605 1.74
REMARK 500 ND2 ASN B 106 O5 NAG B 603 1.79
REMARK 500 ND2 ASN A 481 O5 NAG A 611 1.92
REMARK 500 ND2 ASN A 241 O5 NAG A 606 1.94
REMARK 500 C6 NAG A 608 C1 FUC A 610 2.01
REMARK 500 ND2 ASN B 57 C2 NAG B 602 2.03
REMARK 500 CG ASN B 256 C1 NAG B 608 2.04
REMARK 500 ND2 ASN A 486 O5 NAG A 613 2.07
REMARK 500 ND2 ASN A 106 O5 NAG A 604 2.13
REMARK 500 O4 NAG A 611 O5 NAG A 612 2.13
REMARK 500 CG ASN B 17 C1 NAG B 601 2.14
REMARK 500 OE1 GLU A 80 O HOH A 714 2.15
REMARK 500 CG ASN A 241 C1 NAG A 606 2.16
REMARK 500 CG ASN A 486 C1 NAG A 613 2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 OH TYR A 237 O ARG B 453 1565 2.19
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 PHE A 364 CZ PHE A 364 CE2 -0.118
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 THR A 50 -98.63 -92.37
REMARK 500 ASP A 54 -167.49 104.36
REMARK 500 SER A 89 148.39 -170.27
REMARK 500 ASN A 106 48.86 -153.14
REMARK 500 ALA A 162 75.00 -159.38
REMARK 500 SER A 198 -117.91 65.89
REMARK 500 TYR A 282 -104.98 -71.00
REMARK 500 ASP A 297 -71.79 -127.16
REMARK 500 SER A 362 175.35 -58.11
REMARK 500 ARG A 381 80.73 46.85
REMARK 500 PHE A 398 -56.08 -126.98
REMARK 500 GLU A 482 -82.07 -105.53
REMARK 500 PHE B 43 -2.29 74.85
REMARK 500 ASP B 54 -138.09 -85.66
REMARK 500 SER B 89 148.50 -172.60
REMARK 500 ASN B 106 43.88 -145.10
REMARK 500 ALA B 162 78.74 -162.94
REMARK 500 SER B 198 -111.85 63.00
REMARK 500 TYR B 282 54.70 -90.93
REMARK 500 ASP B 297 -71.35 -136.92
REMARK 500 PHE B 398 -60.40 -127.26
REMARK 500 PRO B 480 44.77 -78.03
REMARK 500 GLU B 506 -73.41 -70.49
REMARK 500 PHE B 525 -52.40 -127.58
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 NAG A 608
REMARK 610 NAG A 609
REMARK 610 FUC A 610
REMARK 610 NAG B 607
REMARK 610 NAG B 610
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 3F9 A 615
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 616
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 617
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 618
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue NDG B 607
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 3F9 B 611
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 612
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 613
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 614
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 615
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 616
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG A 601 bound
REMARK 800 to ASN A 17
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG A
REMARK 800 602 through FUL A 603 bound to ASN A 57
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG A
REMARK 800 604 through NAG A 605 bound to ASN A 106
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG A
REMARK 800 606 through FUC A 607 bound to ASN A 241
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NDG A
REMARK 800 608 through FUC A 610 bound to ASN A 341
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 800 611 through NAG A 612 bound to ASN A 481
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG A
REMARK 800 613 through NAG A 614 bound to ASN A 486
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG B 601 bound
REMARK 800 to ASN B 17
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG B 602 bound
REMARK 800 to ASN B 57
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG B
REMARK 800 603 through NAG B 604 bound to ASN B 106
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG B
REMARK 800 605 through FUL B 606 bound to ASN B 241
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG B 608 bound
REMARK 800 to ASN B 256
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG B 609 bound
REMARK 800 to ASN B 341
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NDG B 610 bound
REMARK 800 to ASN B 481
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4BDS RELATED DB: PDB
REMARK 900 4BDS IS THE SAME PROTEIN COMPLEXED WITH TACRINE
DBREF 4TPK A -27 574 UNP P06276 CHLE_HUMAN 1 602
DBREF 4TPK B -27 574 UNP P06276 CHLE_HUMAN 1 602
SEQRES 1 A 602 MET HIS SER LYS VAL THR ILE ILE CYS ILE ARG PHE LEU
SEQRES 2 A 602 PHE TRP PHE LEU LEU LEU CYS MET LEU ILE GLY LYS SER
SEQRES 3 A 602 HIS THR GLU ASP ASP ILE ILE ILE ALA THR LYS ASN GLY
SEQRES 4 A 602 LYS VAL ARG GLY MET ASN LEU THR VAL PHE GLY GLY THR
SEQRES 5 A 602 VAL THR ALA PHE LEU GLY ILE PRO TYR ALA GLN PRO PRO
SEQRES 6 A 602 LEU GLY ARG LEU ARG PHE LYS LYS PRO GLN SER LEU THR
SEQRES 7 A 602 LYS TRP SER ASP ILE TRP ASN ALA THR LYS TYR ALA ASN
SEQRES 8 A 602 SER CYS CYS GLN ASN ILE ASP GLN SER PHE PRO GLY PHE
SEQRES 9 A 602 HIS GLY SER GLU MET TRP ASN PRO ASN THR ASP LEU SER
SEQRES 10 A 602 GLU ASP CYS LEU TYR LEU ASN VAL TRP ILE PRO ALA PRO
SEQRES 11 A 602 LYS PRO LYS ASN ALA THR VAL LEU ILE TRP ILE TYR GLY
SEQRES 12 A 602 GLY GLY PHE GLN THR GLY THR SER SER LEU HIS VAL TYR
SEQRES 13 A 602 ASP GLY LYS PHE LEU ALA ARG VAL GLU ARG VAL ILE VAL
SEQRES 14 A 602 VAL SER MET ASN TYR ARG VAL GLY ALA LEU GLY PHE LEU
SEQRES 15 A 602 ALA LEU PRO GLY ASN PRO GLU ALA PRO GLY ASN MET GLY
SEQRES 16 A 602 LEU PHE ASP GLN GLN LEU ALA LEU GLN TRP VAL GLN LYS
SEQRES 17 A 602 ASN ILE ALA ALA PHE GLY GLY ASN PRO LYS SER VAL THR
SEQRES 18 A 602 LEU PHE GLY GLU SER ALA GLY ALA ALA SER VAL SER LEU
SEQRES 19 A 602 HIS LEU LEU SER PRO GLY SER HIS SER LEU PHE THR ARG
SEQRES 20 A 602 ALA ILE LEU GLN SER GLY SER PHE ASN ALA PRO TRP ALA
SEQRES 21 A 602 VAL THR SER LEU TYR GLU ALA ARG ASN ARG THR LEU ASN
SEQRES 22 A 602 LEU ALA LYS LEU THR GLY CYS SER ARG GLU ASN GLU THR
SEQRES 23 A 602 GLU ILE ILE LYS CYS LEU ARG ASN LYS ASP PRO GLN GLU
SEQRES 24 A 602 ILE LEU LEU ASN GLU ALA PHE VAL VAL PRO TYR GLY THR
SEQRES 25 A 602 PRO LEU SER VAL ASN PHE GLY PRO THR VAL ASP GLY ASP
SEQRES 26 A 602 PHE LEU THR ASP MET PRO ASP ILE LEU LEU GLU LEU GLY
SEQRES 27 A 602 GLN PHE LYS LYS THR GLN ILE LEU VAL GLY VAL ASN LYS
SEQRES 28 A 602 ASP GLU GLY THR ALA PHE LEU VAL TYR GLY ALA PRO GLY
SEQRES 29 A 602 PHE SER LYS ASP ASN ASN SER ILE ILE THR ARG LYS GLU
SEQRES 30 A 602 PHE GLN GLU GLY LEU LYS ILE PHE PHE PRO GLY VAL SER
SEQRES 31 A 602 GLU PHE GLY LYS GLU SER ILE LEU PHE HIS TYR THR ASP
SEQRES 32 A 602 TRP VAL ASP ASP GLN ARG PRO GLU ASN TYR ARG GLU ALA
SEQRES 33 A 602 LEU GLY ASP VAL VAL GLY ASP TYR ASN PHE ILE CYS PRO
SEQRES 34 A 602 ALA LEU GLU PHE THR LYS LYS PHE SER GLU TRP GLY ASN
SEQRES 35 A 602 ASN ALA PHE PHE TYR TYR PHE GLU HIS ARG SER SER LYS
SEQRES 36 A 602 LEU PRO TRP PRO GLU TRP MET GLY VAL MET HIS GLY TYR
SEQRES 37 A 602 GLU ILE GLU PHE VAL PHE GLY LEU PRO LEU GLU ARG ARG
SEQRES 38 A 602 ASP ASN TYR THR LYS ALA GLU GLU ILE LEU SER ARG SER
SEQRES 39 A 602 ILE VAL LYS ARG TRP ALA ASN PHE ALA LYS TYR GLY ASN
SEQRES 40 A 602 PRO ASN GLU THR GLN ASN ASN SER THR SER TRP PRO VAL
SEQRES 41 A 602 PHE LYS SER THR GLU GLN LYS TYR LEU THR LEU ASN THR
SEQRES 42 A 602 GLU SER THR ARG ILE MET THR LYS LEU ARG ALA GLN GLN
SEQRES 43 A 602 CYS ARG PHE TRP THR SER PHE PHE PRO LYS VAL LEU GLU
SEQRES 44 A 602 MET THR GLY ASN ILE ASP GLU ALA GLU TRP GLU TRP LYS
SEQRES 45 A 602 ALA GLY PHE HIS ARG TRP ASN ASN TYR MET MET ASP TRP
SEQRES 46 A 602 LYS ASN GLN PHE ASN ASP TYR THR SER LYS LYS GLU SER
SEQRES 47 A 602 CYS VAL GLY LEU
SEQRES 1 B 602 MET HIS SER LYS VAL THR ILE ILE CYS ILE ARG PHE LEU
SEQRES 2 B 602 PHE TRP PHE LEU LEU LEU CYS MET LEU ILE GLY LYS SER
SEQRES 3 B 602 HIS THR GLU ASP ASP ILE ILE ILE ALA THR LYS ASN GLY
SEQRES 4 B 602 LYS VAL ARG GLY MET ASN LEU THR VAL PHE GLY GLY THR
SEQRES 5 B 602 VAL THR ALA PHE LEU GLY ILE PRO TYR ALA GLN PRO PRO
SEQRES 6 B 602 LEU GLY ARG LEU ARG PHE LYS LYS PRO GLN SER LEU THR
SEQRES 7 B 602 LYS TRP SER ASP ILE TRP ASN ALA THR LYS TYR ALA ASN
SEQRES 8 B 602 SER CYS CYS GLN ASN ILE ASP GLN SER PHE PRO GLY PHE
SEQRES 9 B 602 HIS GLY SER GLU MET TRP ASN PRO ASN THR ASP LEU SER
SEQRES 10 B 602 GLU ASP CYS LEU TYR LEU ASN VAL TRP ILE PRO ALA PRO
SEQRES 11 B 602 LYS PRO LYS ASN ALA THR VAL LEU ILE TRP ILE TYR GLY
SEQRES 12 B 602 GLY GLY PHE GLN THR GLY THR SER SER LEU HIS VAL TYR
SEQRES 13 B 602 ASP GLY LYS PHE LEU ALA ARG VAL GLU ARG VAL ILE VAL
SEQRES 14 B 602 VAL SER MET ASN TYR ARG VAL GLY ALA LEU GLY PHE LEU
SEQRES 15 B 602 ALA LEU PRO GLY ASN PRO GLU ALA PRO GLY ASN MET GLY
SEQRES 16 B 602 LEU PHE ASP GLN GLN LEU ALA LEU GLN TRP VAL GLN LYS
SEQRES 17 B 602 ASN ILE ALA ALA PHE GLY GLY ASN PRO LYS SER VAL THR
SEQRES 18 B 602 LEU PHE GLY GLU SER ALA GLY ALA ALA SER VAL SER LEU
SEQRES 19 B 602 HIS LEU LEU SER PRO GLY SER HIS SER LEU PHE THR ARG
SEQRES 20 B 602 ALA ILE LEU GLN SER GLY SER PHE ASN ALA PRO TRP ALA
SEQRES 21 B 602 VAL THR SER LEU TYR GLU ALA ARG ASN ARG THR LEU ASN
SEQRES 22 B 602 LEU ALA LYS LEU THR GLY CYS SER ARG GLU ASN GLU THR
SEQRES 23 B 602 GLU ILE ILE LYS CYS LEU ARG ASN LYS ASP PRO GLN GLU
SEQRES 24 B 602 ILE LEU LEU ASN GLU ALA PHE VAL VAL PRO TYR GLY THR
SEQRES 25 B 602 PRO LEU SER VAL ASN PHE GLY PRO THR VAL ASP GLY ASP
SEQRES 26 B 602 PHE LEU THR ASP MET PRO ASP ILE LEU LEU GLU LEU GLY
SEQRES 27 B 602 GLN PHE LYS LYS THR GLN ILE LEU VAL GLY VAL ASN LYS
SEQRES 28 B 602 ASP GLU GLY THR ALA PHE LEU VAL TYR GLY ALA PRO GLY
SEQRES 29 B 602 PHE SER LYS ASP ASN ASN SER ILE ILE THR ARG LYS GLU
SEQRES 30 B 602 PHE GLN GLU GLY LEU LYS ILE PHE PHE PRO GLY VAL SER
SEQRES 31 B 602 GLU PHE GLY LYS GLU SER ILE LEU PHE HIS TYR THR ASP
SEQRES 32 B 602 TRP VAL ASP ASP GLN ARG PRO GLU ASN TYR ARG GLU ALA
SEQRES 33 B 602 LEU GLY ASP VAL VAL GLY ASP TYR ASN PHE ILE CYS PRO
SEQRES 34 B 602 ALA LEU GLU PHE THR LYS LYS PHE SER GLU TRP GLY ASN
SEQRES 35 B 602 ASN ALA PHE PHE TYR TYR PHE GLU HIS ARG SER SER LYS
SEQRES 36 B 602 LEU PRO TRP PRO GLU TRP MET GLY VAL MET HIS GLY TYR
SEQRES 37 B 602 GLU ILE GLU PHE VAL PHE GLY LEU PRO LEU GLU ARG ARG
SEQRES 38 B 602 ASP ASN TYR THR LYS ALA GLU GLU ILE LEU SER ARG SER
SEQRES 39 B 602 ILE VAL LYS ARG TRP ALA ASN PHE ALA LYS TYR GLY ASN
SEQRES 40 B 602 PRO ASN GLU THR GLN ASN ASN SER THR SER TRP PRO VAL
SEQRES 41 B 602 PHE LYS SER THR GLU GLN LYS TYR LEU THR LEU ASN THR
SEQRES 42 B 602 GLU SER THR ARG ILE MET THR LYS LEU ARG ALA GLN GLN
SEQRES 43 B 602 CYS ARG PHE TRP THR SER PHE PHE PRO LYS VAL LEU GLU
SEQRES 44 B 602 MET THR GLY ASN ILE ASP GLU ALA GLU TRP GLU TRP LYS
SEQRES 45 B 602 ALA GLY PHE HIS ARG TRP ASN ASN TYR MET MET ASP TRP
SEQRES 46 B 602 LYS ASN GLN PHE ASN ASP TYR THR SER LYS LYS GLU SER
SEQRES 47 B 602 CYS VAL GLY LEU
HET NAG A 601 14
HET NAG A 602 14
HET FUL A 603 10
HET NAG A 604 14
HET NAG A 605 14
HET NAG A 606 14
HET FUC A 607 10
HET NAG A 608 14
HET NAG A 609 14
HET FUC A 610 10
HET NAG A 611 14
HET NAG A 612 14
HET NAG A 613 14
HET NAG A 614 14
HET 3F9 A 615 33
HET GOL A 616 6
HET EDO A 617 4
HET EDO A 618 4
HET NAG B 601 14
HET NAG B 602 14
HET NAG B 603 14
HET NAG B 604 14
HET NAG B 605 14
HET FUL B 606 10
HET NAG B 607 14
HET NAG B 608 14
HET NAG B 609 14
HET NAG B 610 14
HET 3F9 B 611 33
HET GOL B 612 6
HET GOL B 613 6
HET GOL B 614 6
HET GOL B 615 6
HET EDO B 616 4
HETNAM NAG N-ACETYL-D-GLUCOSAMINE
HETNAM FUL BETA-L-FUCOSE
HETNAM FUC ALPHA-L-FUCOSE
HETNAM 3F9 N-{[(3R)-1-(2,3-DIHYDRO-1H-INDEN-2-YL)PIPERIDIN-3-
HETNAM 2 3F9 YL]METHYL}-N-(2-METHOXYETHYL)NAPHTHALENE-2-CARBOXAMIDE
HETNAM GOL GLYCEROL
HETNAM EDO 1,2-ETHANEDIOL
HETSYN FUL 6-DEOXY-BETA-L-GALACTOSE
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
HETSYN EDO ETHYLENE GLYCOL
FORMUL 3 NAG 20(C8 H15 N O6)
FORMUL 4 FUL 2(C6 H12 O5)
FORMUL 6 FUC 2(C6 H12 O5)
FORMUL 10 3F9 2(C29 H34 N2 O2)
FORMUL 11 GOL 5(C3 H8 O3)
FORMUL 12 EDO 3(C2 H6 O2)
FORMUL 28 HOH *172(H2 O)
HELIX 1 AA1 LEU A 38 ARG A 42 5 5
HELIX 2 AA2 PHE A 76 MET A 81 1 6
HELIX 3 AA3 LEU A 125 ASP A 129 5 5
HELIX 4 AA4 GLY A 130 ARG A 138 1 9
HELIX 5 AA5 GLY A 149 LEU A 154 1 6
HELIX 6 AA6 ASN A 165 ILE A 182 1 18
HELIX 7 AA7 ALA A 183 PHE A 185 5 3
HELIX 8 AA8 SER A 198 SER A 210 1 13
HELIX 9 AA9 SER A 210 SER A 215 1 6
HELIX 10 AB1 SER A 235 THR A 250 1 16
HELIX 11 AB2 ASN A 256 ARG A 265 1 10
HELIX 12 AB3 ASP A 268 LEU A 274 1 7
HELIX 13 AB4 ASN A 275 VAL A 280 5 6
HELIX 14 AB5 MET A 302 LEU A 309 1 8
HELIX 15 AB6 GLY A 326 VAL A 331 1 6
HELIX 16 AB7 THR A 346 PHE A 358 1 13
HELIX 17 AB8 SER A 362 TYR A 373 1 12
HELIX 18 AB9 GLU A 383 PHE A 398 1 16
HELIX 19 AC1 PHE A 398 GLU A 411 1 14
HELIX 20 AC2 PRO A 431 GLY A 435 5 5
HELIX 21 AC3 GLU A 441 PHE A 446 1 6
HELIX 22 AC4 GLY A 447 ASN A 455 5 9
HELIX 23 AC5 THR A 457 GLY A 478 1 22
HELIX 24 AC6 ARG A 515 PHE A 525 1 11
HELIX 25 AC7 PHE A 526 VAL A 529 5 4
HELIX 26 AC8 LEU B 38 ARG B 42 5 5
HELIX 27 AC9 PHE B 76 MET B 81 1 6
HELIX 28 AD1 LEU B 125 ASP B 129 5 5
HELIX 29 AD2 GLY B 130 ARG B 138 1 9
HELIX 30 AD3 GLY B 149 LEU B 154 1 6
HELIX 31 AD4 ASN B 165 ILE B 182 1 18
HELIX 32 AD5 ALA B 183 PHE B 185 5 3
HELIX 33 AD6 SER B 198 SER B 210 1 13
HELIX 34 AD7 PRO B 211 PHE B 217 5 7
HELIX 35 AD8 SER B 235 THR B 250 1 16
HELIX 36 AD9 ASN B 256 ARG B 265 1 10
HELIX 37 AE1 ASP B 268 LEU B 274 1 7
HELIX 38 AE2 ASN B 275 VAL B 280 5 6
HELIX 39 AE3 MET B 302 GLY B 310 1 9
HELIX 40 AE4 GLY B 326 VAL B 331 1 6
HELIX 41 AE5 THR B 346 PHE B 358 1 13
HELIX 42 AE6 SER B 362 TYR B 373 1 12
HELIX 43 AE7 GLU B 383 PHE B 398 1 16
HELIX 44 AE8 PHE B 398 GLU B 411 1 14
HELIX 45 AE9 PRO B 431 GLY B 435 5 5
HELIX 46 AF1 GLU B 441 PHE B 446 1 6
HELIX 47 AF2 GLY B 447 ASN B 455 5 9
HELIX 48 AF3 THR B 457 GLY B 478 1 22
HELIX 49 AF4 ARG B 515 PHE B 525 1 11
HELIX 50 AF5 PHE B 526 VAL B 529 5 4
SHEET 1 AA1 3 ILE A 5 THR A 8 0
SHEET 2 AA1 3 GLY A 11 ARG A 14 -1 O VAL A 13 N ILE A 6
SHEET 3 AA1 3 ILE A 55 ASN A 57 1 O TRP A 56 N ARG A 14
SHEET 1 AA211 MET A 16 VAL A 20 0
SHEET 2 AA211 GLY A 23 PRO A 32 -1 O ALA A 27 N MET A 16
SHEET 3 AA211 TYR A 94 ALA A 101 -1 O LEU A 95 N ILE A 31
SHEET 4 AA211 ILE A 140 MET A 144 -1 O SER A 143 N ASN A 96
SHEET 5 AA211 ALA A 107 ILE A 113 1 N LEU A 110 O ILE A 140
SHEET 6 AA211 GLY A 187 GLU A 197 1 O ASN A 188 N ALA A 107
SHEET 7 AA211 ARG A 219 GLN A 223 1 O ILE A 221 N LEU A 194
SHEET 8 AA211 ILE A 317 ASN A 322 1 O LEU A 318 N LEU A 222
SHEET 9 AA211 ALA A 416 PHE A 421 1 O PHE A 417 N VAL A 319
SHEET 10 AA211 LYS A 499 LEU A 503 1 O LEU A 503 N TYR A 420
SHEET 11 AA211 ILE A 510 THR A 512 -1 O MET A 511 N TYR A 500
SHEET 1 AA3 3 ILE B 5 THR B 8 0
SHEET 2 AA3 3 GLY B 11 ARG B 14 -1 O GLY B 11 N THR B 8
SHEET 3 AA3 3 ILE B 55 ASN B 57 1 O TRP B 56 N LYS B 12
SHEET 1 AA411 MET B 16 VAL B 20 0
SHEET 2 AA411 GLY B 23 PRO B 32 -1 O VAL B 25 N LEU B 18
SHEET 3 AA411 TYR B 94 ALA B 101 -1 O VAL B 97 N PHE B 28
SHEET 4 AA411 ILE B 140 MET B 144 -1 O SER B 143 N ASN B 96
SHEET 5 AA411 ALA B 107 ILE B 113 1 N TRP B 112 O VAL B 142
SHEET 6 AA411 GLY B 187 GLU B 197 1 O THR B 193 N VAL B 109
SHEET 7 AA411 ARG B 219 GLN B 223 1 O ILE B 221 N LEU B 194
SHEET 8 AA411 ILE B 317 ASN B 322 1 O LEU B 318 N LEU B 222
SHEET 9 AA411 ALA B 416 PHE B 421 1 O PHE B 417 N VAL B 319
SHEET 10 AA411 LYS B 499 LEU B 503 1 O LEU B 503 N TYR B 420
SHEET 11 AA411 ILE B 510 THR B 512 -1 O MET B 511 N TYR B 500
SSBOND 1 CYS A 65 CYS A 92 1555 1555 2.04
SSBOND 2 CYS A 252 CYS A 263 1555 1555 2.04
SSBOND 3 CYS A 400 CYS A 519 1555 1555 2.06
SSBOND 4 CYS B 65 CYS B 92 1555 1555 2.05
SSBOND 5 CYS B 252 CYS B 263 1555 1555 2.05
SSBOND 6 CYS B 400 CYS B 519 1555 1555 2.06
LINK ND2 ASN A 17 C1 NAG A 601 1555 1555 1.49
LINK ND2 ASN A 57 C1 NAG A 602 1555 1555 1.47
LINK ND2 ASN A 106 C1 NAG A 604 1555 1555 1.42
LINK ND2 ASN A 241 C1 NAG A 606 1555 1555 1.45
LINK ND2 ASN A 481 C1 NAG A 611 1555 1555 1.41
LINK ND2 ASN A 486 C1 NAG A 613 1555 1555 1.45
LINK ND2 ASN B 17 C1 NAG B 601 1555 1555 1.48
LINK ND2 ASN B 57 C1 NAG B 602 1555 1555 1.47
LINK ND2 ASN B 106 C1 NAG B 603 1555 1555 1.44
LINK ND2 ASN B 241 C1 NAG B 605 1555 1555 1.44
LINK ND2 ASN B 256 C1 NAG B 608 1555 1555 1.46
LINK ND2 ASN B 341 C1 NAG B 609 1555 1555 1.49
LINK O6 NAG A 602 C1 FUL A 603 1555 1555 1.42
LINK O4 NAG A 604 C1 NAG A 605 1555 1555 1.46
LINK O6 NAG A 606 C1 FUC A 607 1555 1555 1.46
LINK O4 NAG A 611 C1 NAG A 612 1555 1555 1.47
LINK O4 NAG A 613 C1 NAG A 614 1555 1555 1.45
LINK O4 NAG B 603 C1 NAG B 604 1555 1555 1.49
LINK O6 NAG B 605 C1 FUL B 606 1555 1555 1.49
CISPEP 1 ALA A 101 PRO A 102 0 4.37
CISPEP 2 GLN A 380 ARG A 381 0 -4.58
CISPEP 3 ALA B 101 PRO B 102 0 4.37
SITE 1 AC1 13 ASN A 68 ILE A 69 ASP A 70 TRP A 82
SITE 2 AC1 13 GLY A 116 GLY A 117 GLU A 197 SER A 198
SITE 3 AC1 13 PHE A 329 TYR A 332 GLY A 439 HOH A 767
SITE 4 AC1 13 HOH A 781
SITE 1 AC2 3 ASN A 228 CYS A 400 PRO A 401
SITE 1 AC3 2 HIS A 77 GLU A 443
SITE 1 AC4 4 LEU A 18 TRP A 98 ASP A 129 LYS A 131
SITE 1 AC5 1 NAG B 605
SITE 1 AC6 10 ASP B 70 TRP B 82 GLY B 116 SER B 198
SITE 2 AC6 10 TRP B 231 LEU B 286 PHE B 329 TYR B 332
SITE 3 AC6 10 HOH B 753 HOH B 785
SITE 1 AC7 5 LEU B 18 TYR B 61 TRP B 98 ASP B 129
SITE 2 AC7 5 LYS B 131
SITE 1 AC8 6 HIS B 372 TYR B 373 THR B 374 ASP B 375
SITE 2 AC8 6 GLN B 518 HOH B 783
SITE 1 AC9 5 SER A 489 ILE B 69 GLN B 71 SER B 72
SITE 2 AC9 5 HOH B 740
SITE 1 AD1 3 HIS B 77 MET B 81 GLU B 443
SITE 1 AD2 2 ARG B 42 LYS B 267
SITE 1 AD3 1 ASN A 17
SITE 1 AD4 3 ASP A 54 ILE A 55 ASN A 57
SITE 1 AD5 4 LYS A 105 ASN A 106 ASN A 188 LYS A 190
SITE 1 AD6 3 ASN A 241 ASN A 245 PHE A 278
SITE 1 AD7 4 PRO A 335 GLY A 336 SER A 338 ASN A 341
SITE 1 AD8 6 TYR A 477 ASN A 481 GLU A 482 GLN A 484
SITE 2 AD8 6 LEU B 88 GLN B 270
SITE 1 AD9 1 ASN A 486
SITE 1 AE1 2 ASN B 17 THR B 24
SITE 1 AE2 4 ARG B 14 ASP B 54 ILE B 55 ASN B 57
SITE 1 AE3 4 ASN B 106 ASN B 188 LYS B 190 HOH B 718
SITE 1 AE4 5 ASN B 241 ASN B 245 LYS B 248 PHE B 278
SITE 2 AE4 5 HOH B 748
SITE 1 AE5 2 ASN B 256 HOH B 745
SITE 1 AE6 5 ASN B 341 ASN B 342 HOH B 746 HOH B 747
SITE 2 AE6 5 HOH B 789
SITE 1 AE7 3 ASN B 481 GLU B 482 HOH B 780
CRYST1 76.600 80.200 231.650 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 0.013055 0.000000 0.000000 0.00000
SCALE2 0.000000 0.012469 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004317 0.00000
TER 4209 LEU A 530
TER 8381 LEU B 530
MASTER 625 0 34 50 28 0 36 6 8938 2 452 94
END |