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HEADER HYDROLASE 22-MAR-18 6G1W
TITLE CRYSTAL STRUCTURE OF TORPEDO CALIFORNICA ACETYLCHOLINESTERASE IN
TITLE 2 COMPLEX WITH 2-{1-[2-(6-CHLORO-1,2,3,4-TETRAHYDROACRIDIN-9-YLAMINO)
TITLE 3 ETHYL]-1H-1,2,3-TRIAZOL-4-YL}-N-[4-(HYDROXY)-3-
TITLE 4 METHOXYBENZYL]ACETAMIDE
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 TORPEDO CALIFORNICA ACETYLCHOLINESTERASE, AD, ALZHEIMER DISEASE,
KEYWDS 2 HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR N.COQUELLE,J.P.COLLETIER
REVDAT 1 04-APR-18 6G1W 0
SPRSDE 04-APR-18 6G1W 6FOV
JRNL AUTH C.GALDEANO,N.COQUELLE,M.CIESLIKIEWICZ-BOUET,M.BARTOLINI,
JRNL AUTH 2 B.PEREZ,M.V.CLOS,I.SILMAN,L.JEAN,J.P.COLLETIER,P.Y.RENARD,
JRNL AUTH 3 D.MUNOZ-TORRERO
JRNL TITL INCREASING POLARITY IN TACRINE AND HUPRINE DERIVATIVES:
JRNL TITL 2 POTENT ANTICHOLINESTERASE AGENTS FOR THE TREATMENT OF
JRNL TITL 3 MYASTHENIA GRAVIS.
JRNL REF MOLECULES V. 23 2018
JRNL REFN ESSN 1420-3049
JRNL PMID 29534488
JRNL DOI 10.3390/MOLECULES23030634
REMARK 2
REMARK 2 RESOLUTION. 1.90 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (1.10.1_2155: ???)
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) : 1.90
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 45.70
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.360
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 3 NUMBER OF REFLECTIONS : 117504
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.190
REMARK 3 R VALUE (WORKING SET) : 0.188
REMARK 3 FREE R VALUE : 0.218
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 5876
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 46.1780 - 5.8999 0.99 3974 210 0.1911 0.2128
REMARK 3 2 5.8999 - 4.6844 1.00 3844 202 0.1524 0.1690
REMARK 3 3 4.6844 - 4.0926 1.00 3801 200 0.1387 0.1551
REMARK 3 4 4.0926 - 3.7186 1.00 3787 200 0.1499 0.1714
REMARK 3 5 3.7186 - 3.4522 1.00 3741 197 0.1703 0.1788
REMARK 3 6 3.4522 - 3.2487 1.00 3755 198 0.1879 0.2253
REMARK 3 7 3.2487 - 3.0860 1.00 3745 197 0.1891 0.2213
REMARK 3 8 3.0860 - 2.9517 1.00 3726 197 0.1947 0.2406
REMARK 3 9 2.9517 - 2.8381 1.00 3724 196 0.1935 0.2326
REMARK 3 10 2.8381 - 2.7402 1.00 3735 197 0.1861 0.2163
REMARK 3 11 2.7402 - 2.6545 1.00 3701 195 0.1840 0.2054
REMARK 3 12 2.6545 - 2.5786 1.00 3736 197 0.1841 0.2092
REMARK 3 13 2.5786 - 2.5108 1.00 3706 195 0.1847 0.2223
REMARK 3 14 2.5108 - 2.4495 1.00 3724 197 0.1822 0.2465
REMARK 3 15 2.4495 - 2.3938 1.00 3688 194 0.1831 0.2235
REMARK 3 16 2.3938 - 2.3429 1.00 3712 196 0.1830 0.2178
REMARK 3 17 2.3429 - 2.2960 1.00 3669 194 0.1883 0.2505
REMARK 3 18 2.2960 - 2.2527 1.00 3710 193 0.2007 0.2335
REMARK 3 19 2.2527 - 2.2125 1.00 3684 194 0.2112 0.2677
REMARK 3 20 2.2125 - 2.1750 1.00 3682 194 0.2203 0.2691
REMARK 3 21 2.1750 - 2.1399 1.00 3671 193 0.2179 0.2646
REMARK 3 22 2.1399 - 2.1070 1.00 3709 194 0.2281 0.2485
REMARK 3 23 2.1070 - 2.0760 1.00 3681 193 0.2245 0.2760
REMARK 3 24 2.0760 - 2.0467 1.00 3681 195 0.2465 0.2834
REMARK 3 25 2.0467 - 2.0191 1.00 3696 191 0.2624 0.3021
REMARK 3 26 2.0191 - 1.9928 1.00 3656 193 0.2790 0.3531
REMARK 3 27 1.9928 - 1.9679 1.00 3681 194 0.3016 0.3434
REMARK 3 28 1.9679 - 1.9442 1.00 3690 193 0.3095 0.3159
REMARK 3 29 1.9442 - 1.9216 1.00 3679 194 0.3362 0.3371
REMARK 3 30 1.9216 - 1.9000 0.99 3640 193 0.3645 0.3742
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) : 0.230
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 26.920
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 9007
REMARK 3 ANGLE : 0.846 12262
REMARK 3 CHIRALITY : 0.053 1286
REMARK 3 PLANARITY : 0.005 1588
REMARK 3 DIHEDRAL : 12.970 5308
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 6G1W COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 22-MAR-18.
REMARK 100 THE DEPOSITION ID IS D_1200009299.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 29-APR-15
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : MASSIF-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.98
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS3 2M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 117742
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.900
REMARK 200 RESOLUTION RANGE LOW (A) : 45.700
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 200 DATA REDUNDANCY : 7.700
REMARK 200 R MERGE (I) : 0.12800
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 8.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.90
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.97
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.4
REMARK 200 DATA REDUNDANCY IN SHELL : 7.50
REMARK 200 R MERGE FOR SHELL (I) : 1.28600
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 1.000
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: 2XI4
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 56.36
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.82
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 30% PEG 200/50 MM 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 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 45.91000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 75.83500
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 53.40500
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 75.83500
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 45.91000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 53.40500
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: 3560 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 39480 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -35.0 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 MET A -20
REMARK 465 ASN A -19
REMARK 465 LEU A -18
REMARK 465 LEU A -17
REMARK 465 VAL A -16
REMARK 465 THR A -15
REMARK 465 SER A -14
REMARK 465 SER A -13
REMARK 465 LEU A -12
REMARK 465 GLY A -11
REMARK 465 VAL A -10
REMARK 465 LEU A -9
REMARK 465 LEU A -8
REMARK 465 HIS A -7
REMARK 465 LEU A -6
REMARK 465 VAL A -5
REMARK 465 VAL A -4
REMARK 465 LEU A -3
REMARK 465 CYS A -2
REMARK 465 GLN A -1
REMARK 465 ALA A 0
REMARK 465 ASP A 1
REMARK 465 ASP A 2
REMARK 465 HIS A 3
REMARK 465 GLN A 488
REMARK 465 GLU A 489
REMARK 465 ALA A 536
REMARK 465 CYS A 537
REMARK 465 ASP A 538
REMARK 465 GLY A 539
REMARK 465 GLU A 540
REMARK 465 LEU A 541
REMARK 465 SER A 542
REMARK 465 SER A 543
REMARK 465 SER A 544
REMARK 465 GLY A 545
REMARK 465 THR A 546
REMARK 465 SER A 547
REMARK 465 SER A 548
REMARK 465 SER A 549
REMARK 465 LYS A 550
REMARK 465 GLY A 551
REMARK 465 ILE A 552
REMARK 465 ILE A 553
REMARK 465 PHE A 554
REMARK 465 TYR A 555
REMARK 465 VAL A 556
REMARK 465 LEU A 557
REMARK 465 PHE A 558
REMARK 465 SER A 559
REMARK 465 ILE A 560
REMARK 465 LEU A 561
REMARK 465 TYR A 562
REMARK 465 LEU A 563
REMARK 465 ILE A 564
REMARK 465 PHE A 565
REMARK 465 MET B -20
REMARK 465 ASN B -19
REMARK 465 LEU B -18
REMARK 465 LEU B -17
REMARK 465 VAL B -16
REMARK 465 THR B -15
REMARK 465 SER B -14
REMARK 465 SER B -13
REMARK 465 LEU B -12
REMARK 465 GLY B -11
REMARK 465 VAL B -10
REMARK 465 LEU B -9
REMARK 465 LEU B -8
REMARK 465 HIS B -7
REMARK 465 LEU B -6
REMARK 465 VAL B -5
REMARK 465 VAL B -4
REMARK 465 LEU B -3
REMARK 465 CYS B -2
REMARK 465 GLN B -1
REMARK 465 ALA B 0
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 465 ASP B 538
REMARK 465 GLY B 539
REMARK 465 GLU B 540
REMARK 465 LEU B 541
REMARK 465 SER B 542
REMARK 465 SER B 543
REMARK 465 SER B 544
REMARK 465 GLY B 545
REMARK 465 THR B 546
REMARK 465 SER B 547
REMARK 465 SER B 548
REMARK 465 SER B 549
REMARK 465 LYS B 550
REMARK 465 GLY B 551
REMARK 465 ILE B 552
REMARK 465 ILE B 553
REMARK 465 PHE B 554
REMARK 465 TYR B 555
REMARK 465 VAL B 556
REMARK 465 LEU B 557
REMARK 465 PHE B 558
REMARK 465 SER B 559
REMARK 465 ILE B 560
REMARK 465 LEU B 561
REMARK 465 TYR B 562
REMARK 465 LEU B 563
REMARK 465 ILE B 564
REMARK 465 PHE B 565
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 LYS A 413 CD CE NZ
REMARK 470 LYS A 454 CE NZ
REMARK 470 HIS A 486 ND1 CD2 CE1 NE2
REMARK 470 LYS A 511 CE NZ
REMARK 470 ARG B 46 NE CZ NH1 NH2
REMARK 470 LYS B 413 CD CE NZ
REMARK 470 LYS B 454 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 HOH A 1106 O HOH A 1136 2.12
REMARK 500 O HOH B 1067 O HOH B 1142 2.13
REMARK 500 O PRO A 485 O HOH A 701 2.14
REMARK 500 NE2 GLN B 526 O HOH B 701 2.15
REMARK 500 O35 E0Z A 604 O HOH A 702 2.16
REMARK 500 O HOH A 1051 O HOH A 1065 2.16
REMARK 500 NH1 ARG A 468 O HOH A 703 2.16
REMARK 500 O HOH B 1016 O HOH B 1143 2.17
REMARK 500 O HOH A 1018 O HOH A 1050 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 PHE A 45 -7.83 79.50
REMARK 500 ALA A 60 45.73 -107.08
REMARK 500 CYS A 94 14.88 -141.28
REMARK 500 SER A 108 71.73 -156.07
REMARK 500 SER A 200 -125.49 56.63
REMARK 500 GLU A 299 -68.40 -125.93
REMARK 500 ASP A 380 51.55 -159.84
REMARK 500 VAL A 400 -59.72 -126.75
REMARK 500 PRO A 485 65.40 -66.86
REMARK 500 HIS A 486 144.94 168.95
REMARK 500 GLN A 526 -56.53 -123.39
REMARK 500 SER B 25 -159.56 -137.36
REMARK 500 PHE B 45 -8.04 79.41
REMARK 500 ALA B 60 47.05 -107.35
REMARK 500 SER B 108 78.27 -153.63
REMARK 500 SER B 200 -124.36 56.83
REMARK 500 GLU B 299 -72.08 -123.90
REMARK 500 THR B 317 -158.63 -153.21
REMARK 500 ASP B 380 50.71 -153.24
REMARK 500 VAL B 400 -60.21 -123.55
REMARK 500 HIS B 486 -4.61 71.01
REMARK 500 ASN B 506 -169.77 -161.03
REMARK 500 ARG B 515 70.79 57.78
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH A1147 DISTANCE = 6.09 ANGSTROMS
REMARK 525 HOH B1164 DISTANCE = 5.82 ANGSTROMS
REMARK 525 HOH B1165 DISTANCE = 5.84 ANGSTROMS
REMARK 525 HOH B1166 DISTANCE = 6.21 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue E0Z A 604
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 605
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue E0Z B 604
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL B 605
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL B 606
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
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: AC7
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: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG A 603 bound
REMARK 800 to ASN A 457
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
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: AD1
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 800
REMARK 800 SITE_IDENTIFIER: AD2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG B 603 bound
REMARK 800 to ASN B 457
DBREF 6G1W A -20 565 UNP P04058 ACES_TETCF 1 586
DBREF 6G1W B -20 565 UNP P04058 ACES_TETCF 1 586
SEQRES 1 A 586 MET ASN LEU LEU VAL THR SER SER LEU GLY VAL LEU LEU
SEQRES 2 A 586 HIS LEU VAL VAL LEU CYS GLN ALA ASP ASP HIS SER GLU
SEQRES 3 A 586 LEU LEU VAL ASN THR LYS SER GLY LYS VAL MET GLY THR
SEQRES 4 A 586 ARG VAL PRO VAL LEU SER SER HIS ILE SER ALA PHE LEU
SEQRES 5 A 586 GLY ILE PRO PHE ALA GLU PRO PRO VAL GLY ASN MET ARG
SEQRES 6 A 586 PHE ARG ARG PRO GLU PRO LYS LYS PRO TRP SER GLY VAL
SEQRES 7 A 586 TRP ASN ALA SER THR TYR PRO ASN ASN CYS GLN GLN TYR
SEQRES 8 A 586 VAL ASP GLU GLN PHE PRO GLY PHE SER GLY SER GLU MET
SEQRES 9 A 586 TRP ASN PRO ASN ARG GLU MET SER GLU ASP CYS LEU TYR
SEQRES 10 A 586 LEU ASN ILE TRP VAL PRO SER PRO ARG PRO LYS SER THR
SEQRES 11 A 586 THR VAL MET VAL TRP ILE TYR GLY GLY GLY PHE TYR SER
SEQRES 12 A 586 GLY SER SER THR LEU ASP VAL TYR ASN GLY LYS TYR LEU
SEQRES 13 A 586 ALA TYR THR GLU GLU VAL VAL LEU VAL SER LEU SER TYR
SEQRES 14 A 586 ARG VAL GLY ALA PHE GLY PHE LEU ALA LEU HIS GLY SER
SEQRES 15 A 586 GLN GLU ALA PRO GLY ASN VAL GLY LEU LEU ASP GLN ARG
SEQRES 16 A 586 MET ALA LEU GLN TRP VAL HIS ASP ASN ILE GLN PHE PHE
SEQRES 17 A 586 GLY GLY ASP PRO LYS THR VAL THR ILE PHE GLY GLU SER
SEQRES 18 A 586 ALA GLY GLY ALA SER VAL GLY MET HIS ILE LEU SER PRO
SEQRES 19 A 586 GLY SER ARG ASP LEU PHE ARG ARG ALA ILE LEU GLN SER
SEQRES 20 A 586 GLY SER PRO ASN CYS PRO TRP ALA SER VAL SER VAL ALA
SEQRES 21 A 586 GLU GLY ARG ARG ARG ALA VAL GLU LEU GLY ARG ASN LEU
SEQRES 22 A 586 ASN CYS ASN LEU ASN SER ASP GLU GLU LEU ILE HIS CYS
SEQRES 23 A 586 LEU ARG GLU LYS LYS PRO GLN GLU LEU ILE ASP VAL GLU
SEQRES 24 A 586 TRP ASN VAL LEU PRO PHE ASP SER ILE PHE ARG PHE SER
SEQRES 25 A 586 PHE VAL PRO VAL ILE ASP GLY GLU PHE PHE PRO THR SER
SEQRES 26 A 586 LEU GLU SER MET LEU ASN SER GLY ASN PHE LYS LYS THR
SEQRES 27 A 586 GLN ILE LEU LEU GLY VAL ASN LYS ASP GLU GLY SER PHE
SEQRES 28 A 586 PHE LEU LEU TYR GLY ALA PRO GLY PHE SER LYS ASP SER
SEQRES 29 A 586 GLU SER LYS ILE SER ARG GLU ASP PHE MET SER GLY VAL
SEQRES 30 A 586 LYS LEU SER VAL PRO HIS ALA ASN ASP LEU GLY LEU ASP
SEQRES 31 A 586 ALA VAL THR LEU GLN TYR THR ASP TRP MET ASP ASP ASN
SEQRES 32 A 586 ASN GLY ILE LYS ASN ARG ASP GLY LEU ASP ASP ILE VAL
SEQRES 33 A 586 GLY ASP HIS ASN VAL ILE CYS PRO LEU MET HIS PHE VAL
SEQRES 34 A 586 ASN LYS TYR THR LYS PHE GLY ASN GLY THR TYR LEU TYR
SEQRES 35 A 586 PHE PHE ASN HIS ARG ALA SER ASN LEU VAL TRP PRO GLU
SEQRES 36 A 586 TRP MET GLY VAL ILE HIS GLY TYR GLU ILE GLU PHE VAL
SEQRES 37 A 586 PHE GLY LEU PRO LEU VAL LYS GLU LEU ASN TYR THR ALA
SEQRES 38 A 586 GLU GLU GLU ALA LEU SER ARG ARG ILE MET HIS TYR TRP
SEQRES 39 A 586 ALA THR PHE ALA LYS THR GLY ASN PRO ASN GLU PRO HIS
SEQRES 40 A 586 SER GLN GLU SER LYS TRP PRO LEU PHE THR THR LYS GLU
SEQRES 41 A 586 GLN LYS PHE ILE ASP LEU ASN THR GLU PRO MET LYS VAL
SEQRES 42 A 586 HIS GLN ARG LEU ARG VAL GLN MET CYS VAL PHE TRP ASN
SEQRES 43 A 586 GLN PHE LEU PRO LYS LEU LEU ASN ALA THR ALA CYS ASP
SEQRES 44 A 586 GLY GLU LEU SER SER SER GLY THR SER SER SER LYS GLY
SEQRES 45 A 586 ILE ILE PHE TYR VAL LEU PHE SER ILE LEU TYR LEU ILE
SEQRES 46 A 586 PHE
SEQRES 1 B 586 MET ASN LEU LEU VAL THR SER SER LEU GLY VAL LEU LEU
SEQRES 2 B 586 HIS LEU VAL VAL LEU CYS GLN ALA ASP ASP HIS SER GLU
SEQRES 3 B 586 LEU LEU VAL ASN THR LYS SER GLY LYS VAL MET GLY THR
SEQRES 4 B 586 ARG VAL PRO VAL LEU SER SER HIS ILE SER ALA PHE LEU
SEQRES 5 B 586 GLY ILE PRO PHE ALA GLU PRO PRO VAL GLY ASN MET ARG
SEQRES 6 B 586 PHE ARG ARG PRO GLU PRO LYS LYS PRO TRP SER GLY VAL
SEQRES 7 B 586 TRP ASN ALA SER THR TYR PRO ASN ASN CYS GLN GLN TYR
SEQRES 8 B 586 VAL ASP GLU GLN PHE PRO GLY PHE SER GLY SER GLU MET
SEQRES 9 B 586 TRP ASN PRO ASN ARG GLU MET SER GLU ASP CYS LEU TYR
SEQRES 10 B 586 LEU ASN ILE TRP VAL PRO SER PRO ARG PRO LYS SER THR
SEQRES 11 B 586 THR VAL MET VAL TRP ILE TYR GLY GLY GLY PHE TYR SER
SEQRES 12 B 586 GLY SER SER THR LEU ASP VAL TYR ASN GLY LYS TYR LEU
SEQRES 13 B 586 ALA TYR THR GLU GLU VAL VAL LEU VAL SER LEU SER TYR
SEQRES 14 B 586 ARG VAL GLY ALA PHE GLY PHE LEU ALA LEU HIS GLY SER
SEQRES 15 B 586 GLN GLU ALA PRO GLY ASN VAL GLY LEU LEU ASP GLN ARG
SEQRES 16 B 586 MET ALA LEU GLN TRP VAL HIS ASP ASN ILE GLN PHE PHE
SEQRES 17 B 586 GLY GLY ASP PRO LYS THR VAL THR ILE PHE GLY GLU SER
SEQRES 18 B 586 ALA GLY GLY ALA SER VAL GLY MET HIS ILE LEU SER PRO
SEQRES 19 B 586 GLY SER ARG ASP LEU PHE ARG ARG ALA ILE LEU GLN SER
SEQRES 20 B 586 GLY SER PRO ASN CYS PRO TRP ALA SER VAL SER VAL ALA
SEQRES 21 B 586 GLU GLY ARG ARG ARG ALA VAL GLU LEU GLY ARG ASN LEU
SEQRES 22 B 586 ASN CYS ASN LEU ASN SER ASP GLU GLU LEU ILE HIS CYS
SEQRES 23 B 586 LEU ARG GLU LYS LYS PRO GLN GLU LEU ILE ASP VAL GLU
SEQRES 24 B 586 TRP ASN VAL LEU PRO PHE ASP SER ILE PHE ARG PHE SER
SEQRES 25 B 586 PHE VAL PRO VAL ILE ASP GLY GLU PHE PHE PRO THR SER
SEQRES 26 B 586 LEU GLU SER MET LEU ASN SER GLY ASN PHE LYS LYS THR
SEQRES 27 B 586 GLN ILE LEU LEU GLY VAL ASN LYS ASP GLU GLY SER PHE
SEQRES 28 B 586 PHE LEU LEU TYR GLY ALA PRO GLY PHE SER LYS ASP SER
SEQRES 29 B 586 GLU SER LYS ILE SER ARG GLU ASP PHE MET SER GLY VAL
SEQRES 30 B 586 LYS LEU SER VAL PRO HIS ALA ASN ASP LEU GLY LEU ASP
SEQRES 31 B 586 ALA VAL THR LEU GLN TYR THR ASP TRP MET ASP ASP ASN
SEQRES 32 B 586 ASN GLY ILE LYS ASN ARG ASP GLY LEU ASP ASP ILE VAL
SEQRES 33 B 586 GLY ASP HIS ASN VAL ILE CYS PRO LEU MET HIS PHE VAL
SEQRES 34 B 586 ASN LYS TYR THR LYS PHE GLY ASN GLY THR TYR LEU TYR
SEQRES 35 B 586 PHE PHE ASN HIS ARG ALA SER ASN LEU VAL TRP PRO GLU
SEQRES 36 B 586 TRP MET GLY VAL ILE HIS GLY TYR GLU ILE GLU PHE VAL
SEQRES 37 B 586 PHE GLY LEU PRO LEU VAL LYS GLU LEU ASN TYR THR ALA
SEQRES 38 B 586 GLU GLU GLU ALA LEU SER ARG ARG ILE MET HIS TYR TRP
SEQRES 39 B 586 ALA THR PHE ALA LYS THR GLY ASN PRO ASN GLU PRO HIS
SEQRES 40 B 586 SER GLN GLU SER LYS TRP PRO LEU PHE THR THR LYS GLU
SEQRES 41 B 586 GLN LYS PHE ILE ASP LEU ASN THR GLU PRO MET LYS VAL
SEQRES 42 B 586 HIS GLN ARG LEU ARG VAL GLN MET CYS VAL PHE TRP ASN
SEQRES 43 B 586 GLN PHE LEU PRO LYS LEU LEU ASN ALA THR ALA CYS ASP
SEQRES 44 B 586 GLY GLU LEU SER SER SER GLY THR SER SER SER LYS GLY
SEQRES 45 B 586 ILE ILE PHE TYR VAL LEU PHE SER ILE LEU TYR LEU ILE
SEQRES 46 B 586 PHE
HET NAG A 601 14
HET NAG A 602 14
HET NAG A 603 14
HET E0Z A 604 37
HET CL A 605 1
HET CL A 606 1
HET CL A 607 1
HET NAG B 601 14
HET NAG B 602 14
HET NAG B 603 14
HET E0Z B 604 37
HET CL B 605 1
HET CL B 606 1
HETNAM NAG N-ACETYL-D-GLUCOSAMINE
HETNAM E0Z 2-[1-[2-[(3-CHLORANYLACRIDIN-9-YL)AMINO]ETHYL]-1,2,3-
HETNAM 2 E0Z TRIAZOL-4-YL]-~{N}-[(3-METHOXY-4-OXIDANYL-PHENYL)
HETNAM 3 E0Z METHYL]ETHANAMIDE
HETNAM CL CHLORIDE ION
FORMUL 3 NAG 6(C8 H15 N O6)
FORMUL 6 E0Z 2(C27 H25 CL N6 O3)
FORMUL 7 CL 5(CL 1-)
FORMUL 16 HOH *913(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 GLY A 151 LEU A 156 1 6
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 ASP A 276 1 7
HELIX 13 AB4 VAL A 277 LEU A 282 5 6
HELIX 14 AB5 SER A 304 GLY A 312 1 9
HELIX 15 AB6 GLY A 328 ALA A 336 1 9
HELIX 16 AB7 SER A 348 VAL A 360 1 13
HELIX 17 AB8 ASN A 364 THR A 376 1 13
HELIX 18 AB9 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 SER B 212 ASP B 217 1 6
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 ASN B 533 1 8
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 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 VAL A 101 -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 ASP A 190 N THR A 109
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
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
SHEET 1 AA4 3 LEU B 7 THR B 10 0
SHEET 2 AA4 3 GLY B 13 MET B 16 -1 O VAL B 15 N VAL B 8
SHEET 3 AA4 3 VAL B 57 ASN B 59 1 O TRP B 58 N LYS B 14
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 ILE B 99 N PHE B 30
SHEET 4 AA511 VAL B 142 SER B 145 -1 O LEU B 143 N TRP B 100
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 LEU B 224
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 LEU B 505 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 2.05
SSBOND 2 CYS A 254 CYS A 265 1555 1555 2.04
SSBOND 3 CYS A 402 CYS A 521 1555 1555 2.06
SSBOND 4 CYS B 67 CYS B 94 1555 1555 2.06
SSBOND 5 CYS B 254 CYS B 265 1555 1555 2.04
SSBOND 6 CYS B 402 CYS B 521 1555 1555 2.04
LINK ND2 ASN A 59 C1 NAG A 601 1555 1555 1.45
LINK ND2 ASN A 416 C1 NAG A 602 1555 1555 1.52
LINK ND2 ASN A 457 C1 NAG A 603 1555 1555 1.51
LINK ND2 ASN B 59 C1 NAG B 601 1555 1555 1.44
LINK ND2 ASN B 416 C1 NAG B 602 1555 1555 1.49
LINK ND2 ASN B 457 C1 NAG B 603 1555 1555 1.44
CISPEP 1 SER A 103 PRO A 104 0 6.70
CISPEP 2 SER B 103 PRO B 104 0 4.89
SITE 1 AC1 20 TRP A 84 GLY A 118 TYR A 121 GLU A 199
SITE 2 AC1 20 LEU A 282 SER A 286 ILE A 287 PHE A 288
SITE 3 AC1 20 ARG A 289 PHE A 290 PHE A 330 PHE A 331
SITE 4 AC1 20 TYR A 334 TRP A 432 MET A 436 HIS A 440
SITE 5 AC1 20 HOH A 702 HOH A 721 HOH A 729 HOH A 800
SITE 1 AC2 2 TYR A 134 HOH A 935
SITE 1 AC3 13 TRP B 84 GLY B 118 TYR B 121 GLU B 199
SITE 2 AC3 13 SER B 286 PHE B 330 TYR B 334 TRP B 432
SITE 3 AC3 13 HIS B 440 HOH B 708 HOH B 778 HOH B 859
SITE 4 AC3 13 HOH B 904
SITE 1 AC4 2 THR B 497 HOH B1045
SITE 1 AC5 1 TYR B 134
SITE 1 AC6 4 ASN A 59 SER A 61 HOH A 724 HOH A1007
SITE 1 AC7 2 ASN A 416 HOH A 726
SITE 1 AC8 3 ASN A 457 HOH A 707 HOH A 754
SITE 1 AC9 4 ASN B 59 SER B 61 HOH B 704 HOH B 719
SITE 1 AD1 2 ASN B 416 HOH B 811
SITE 1 AD2 1 ASN B 457
CRYST1 91.820 106.810 151.670 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 0.010891 0.000000 0.000000 0.00000
SCALE2 0.000000 0.009362 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006593 0.00000
TER 4270 THR A 535
TER 8566 THR B 535
MASTER 476 0 13 50 32 0 18 6 9526 2 176 92
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