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HEADER HYDROLASE 25-SEP-15 5DYW
TITLE CRYSTAL STRUCTURE OF HUMAN BUTYRYLCHOLINESTERASE IN COMPLEX WITH N-
TITLE 2 ((1-BENZYLPIPERIDIN-3-YL)METHYL)-N-(2-METHOXYETHYL)NAPHTHALENE-2-
TITLE 3 SULFONAMIDE
CAVEAT 5DYW 5HF A 601 HAS WRONG CHIRALITY AT ATOM C07 NAG A 621 HAS
CAVEAT 2 5DYW WRONG CHIRALITY AT ATOM C1 NAG A 622 HAS WRONG CHIRALITY AT
CAVEAT 3 5DYW ATOM C1 NAG A 625 HAS WRONG CHIRALITY AT ATOM C1 NAG A 628
CAVEAT 4 5DYW HAS WRONG CHIRALITY AT ATOM C1 NAG B 614 HAS WRONG
CAVEAT 5 5DYW CHIRALITY AT ATOM C1 NAG B 618 HAS WRONG CHIRALITY AT ATOM
CAVEAT 6 5DYW 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: DROSOPHILA MELANOGASTER;
SOURCE 7 EXPRESSION_SYSTEM_COMMON: FRUIT FLY;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 7227
KEYWDS HYDROLASE, HUMAN BUTYRYLCHOLINESTERASE AD ALZHEIMER DISEASE
KEYWDS 2 SULFONAMIDE
EXPDTA X-RAY DIFFRACTION
AUTHOR N.COQUELLE,B.BRUS,J.P.COLLETIER
REVDAT 1 18-JAN-17 5DYW 0
JRNL AUTH U.KOSAK,B.BRUS,D.KNEZ,R.SINK,S.ZAKELJ,J.TRONTELJ,A.PISLAR,
JRNL AUTH 2 J.SLENC,M.GOBEC,M.ZIVIN,L.TRATNJEK,M.PERSE,K.SAAT,A.PODKOWA,
JRNL AUTH 3 B.FILIPEK,F.NACHON,X.BRAZZOLOTTO,A.WIECKOWSKA,B.MALAWSKA,
JRNL AUTH 4 J.STOJAN,I.M.RASCAN,J.KOS,N.COQUELLE,J.P.COLLETIER,S.GOBEC
JRNL TITL DEVELOPMENT OF AN IN-VIVO ACTIVE REVERSIBLE
JRNL TITL 2 BUTYRYLCHOLINESTERASE INHIBITOR.
JRNL REF SCI REP V. 6 39495 2016
JRNL REFN ESSN 2045-2322
JRNL PMID 28000737
JRNL DOI 10.1038/SREP39495
REMARK 2
REMARK 2 RESOLUTION. 2.50 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (1.10_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 : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 46.02
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.360
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 45684
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.191
REMARK 3 R VALUE (WORKING SET) : 0.190
REMARK 3 FREE R VALUE : 0.217
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 2284
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 46.0242 - 6.2947 1.00 2915 154 0.1797 0.1799
REMARK 3 2 6.2947 - 4.9982 1.00 2779 146 0.1830 0.1958
REMARK 3 3 4.9982 - 4.3670 1.00 2754 145 0.1492 0.1745
REMARK 3 4 4.3670 - 3.9680 1.00 2720 143 0.1526 0.1650
REMARK 3 5 3.9680 - 3.6837 1.00 2718 143 0.1620 0.2067
REMARK 3 6 3.6837 - 3.4666 1.00 2715 143 0.1762 0.1823
REMARK 3 7 3.4666 - 3.2930 1.00 2680 141 0.1867 0.2390
REMARK 3 8 3.2930 - 3.1497 1.00 2694 142 0.2031 0.2833
REMARK 3 9 3.1497 - 3.0285 1.00 2704 142 0.2174 0.2422
REMARK 3 10 3.0285 - 2.9240 1.00 2693 142 0.2141 0.2590
REMARK 3 11 2.9240 - 2.8326 1.00 2684 141 0.2268 0.2736
REMARK 3 12 2.8326 - 2.7516 1.00 2681 141 0.2358 0.2945
REMARK 3 13 2.7516 - 2.6792 1.00 2664 140 0.2505 0.2798
REMARK 3 14 2.6792 - 2.6138 1.00 2664 141 0.2580 0.3208
REMARK 3 15 2.6138 - 2.5544 1.00 2650 139 0.2767 0.2882
REMARK 3 16 2.5544 - 2.5001 1.00 2685 141 0.3036 0.3493
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) : 0.310
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 22.360
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 9209
REMARK 3 ANGLE : 0.885 12438
REMARK 3 CHIRALITY : 0.051 1366
REMARK 3 PLANARITY : 0.005 1544
REMARK 3 DIHEDRAL : 15.745 5312
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 5DYW COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 25-SEP-15.
REMARK 100 THE DEPOSITION ID IS D_1000214053.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 28-JUL-14
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 : ID14-4
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.93903
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 45699
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.500
REMARK 200 RESOLUTION RANGE LOW (A) : 48.200
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 7.400
REMARK 200 R MERGE (I) : 0.15960
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 12.4800
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.55
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.59
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 1.37000
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: 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 (%): 54.44
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.70
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M AMMONIUM ACETATE, 12%
REMARK 280 POLYETHYLENE GLYCOL 4000., PH 7.4, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 293K
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 36.10700
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 113.32500
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 39.43150
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 113.32500
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 36.10700
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 39.43150
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: 14670 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 40490 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 82.0 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 THR A 0
REMARK 465 GLU A 1
REMARK 465 ASP A 2
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 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 GLN A 380 CG CD OE1 NE2
REMARK 470 ARG A 453 CG CD NE CZ NH1 NH2
REMARK 470 ASN B 485 CG OD1 ND2
REMARK 470 ASN B 486 CG OD1 ND2
REMARK 470 GLU B 506 CG CD OE1 OE2
REMARK 470 SER B 507 CB OG
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 GLU A 506 CD OE1 OE2
REMARK 480 SER B 53 CB OG
REMARK 480 ASN B 485 CB
REMARK 480 ARG B 509 NE CZ NH1 NH2
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 B 106 O5 NAG B 614 1.69
REMARK 500 C6 NAG B 618 C1 FUL B 620 1.79
REMARK 500 ND2 ASN B 256 O5 NAG B 618 1.93
REMARK 500 NH2 ARG A 386 O2 EDO A 610 1.94
REMARK 500 O HOH A 812 O HOH A 824 2.00
REMARK 500 O4 NAG A 626 O5 NAG A 627 2.05
REMARK 500 ND2 ASN A 17 C2 NAG A 615 2.06
REMARK 500 ND2 ASN A 57 O5 NAG A 617 2.07
REMARK 500 NZ LYS B 44 OE1 GLU B 161 2.08
REMARK 500 O4 NAG A 628 O5 NAG A 629 2.10
REMARK 500 O PHE B 217 NZ LYS B 313 2.12
REMARK 500 ND2 ASN B 57 C2 NAG B 613 2.13
REMARK 500 ND2 ASN B 241 O5 NAG B 615 2.15
REMARK 500 O6 NAG A 628 C2 FUL A 630 2.17
REMARK 500 ND2 ASN A 17 O5 NAG A 615 2.17
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 43 -4.56 80.01
REMARK 500 THR A 50 -77.90 -85.87
REMARK 500 ASP A 54 -159.13 -109.70
REMARK 500 GLN A 67 147.88 -170.33
REMARK 500 ASN A 106 51.30 -158.73
REMARK 500 ALA A 162 72.17 -161.88
REMARK 500 SER A 198 -118.79 56.54
REMARK 500 ASP A 297 -72.01 -113.60
REMARK 500 GLN A 380 120.80 -172.74
REMARK 500 ARG A 381 76.75 57.50
REMARK 500 PHE A 398 -61.38 -132.18
REMARK 500 PRO A 480 45.86 -81.03
REMARK 500 GLU A 482 -72.05 -106.94
REMARK 500 PHE A 525 -52.17 -129.61
REMARK 500 LYS B 9 3.82 -68.66
REMARK 500 PRO B 37 62.60 -69.90
REMARK 500 PHE B 43 -3.59 81.04
REMARK 500 ASP B 54 -156.16 -84.36
REMARK 500 GLN B 67 147.81 -179.20
REMARK 500 CYS B 92 10.57 -143.30
REMARK 500 ALA B 162 79.47 -158.08
REMARK 500 ASN B 165 19.68 54.84
REMARK 500 SER B 198 -112.50 58.15
REMARK 500 ASP B 297 -68.86 -108.91
REMARK 500 THR B 315 -177.16 -171.55
REMARK 500 ASP B 378 98.72 -167.07
REMARK 500 PHE B 398 -54.77 -132.74
REMARK 500 GLU B 411 2.63 -61.54
REMARK 500 ASP B 454 -156.98 -95.92
REMARK 500 PRO B 480 44.86 -74.54
REMARK 500 ASN B 486 66.08 -100.86
REMARK 500 THR B 496 -60.38 -91.70
REMARK 500 GLU B 506 -75.42 -62.56
REMARK 500 PRO B 527 -6.02 -58.72
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 A 866 DISTANCE = 6.41 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 5HF A 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 602
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 603
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 604
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 605
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 606
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 607
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 608
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 609
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 610
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 611
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 612
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 613
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PG4 A 614
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 5HF B 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 602
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 603
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 604
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 605
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 606
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 607
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 608
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 609
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL B 610
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL B 611
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG A
REMARK 800 615 through NAG A 616 bound to ASN A 17
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG A
REMARK 800 617 through FUC A 619 bound to ASN A 57
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG A
REMARK 800 620 through NAG A 621 bound to ASN A 106
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG A
REMARK 800 622 through FUC A 624 bound to ASN A 241
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG A 625 bound
REMARK 800 to ASN A 341
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG A
REMARK 800 626 through NAG A 627 bound to ASN A 481
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG A
REMARK 800 628 through FUL A 630 bound to ASN A 486
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG B 612 bound
REMARK 800 to ASN B 17
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG B 613 bound
REMARK 800 to ASN B 57
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG B 614 bound
REMARK 800 to ASN B 106
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG B
REMARK 800 615 through FUL B 617 bound to ASN B 241
REMARK 800
REMARK 800 SITE_IDENTIFIER: AG1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG B
REMARK 800 618 through FUL B 620 bound to ASN B 256
REMARK 800
REMARK 800 SITE_IDENTIFIER: AG2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG B 621 bound
REMARK 800 to ASN B 341
REMARK 800
REMARK 800 SITE_IDENTIFIER: AG3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG B
REMARK 800 622 through FUL B 624 bound to ASN B 455
REMARK 800
REMARK 800 SITE_IDENTIFIER: AG4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG B 625 bound
REMARK 800 to ASN B 481
DBREF 5DYW A 0 529 UNP P06276 CHLE_HUMAN 28 557
DBREF 5DYW B 0 529 UNP P06276 CHLE_HUMAN 28 557
SEQRES 1 A 530 THR GLU ASP ASP ILE ILE ILE ALA THR LYS ASN GLY LYS
SEQRES 2 A 530 VAL ARG GLY MET ASN LEU THR VAL PHE GLY GLY THR VAL
SEQRES 3 A 530 THR ALA PHE LEU GLY ILE PRO TYR ALA GLN PRO PRO LEU
SEQRES 4 A 530 GLY ARG LEU ARG PHE LYS LYS PRO GLN SER LEU THR LYS
SEQRES 5 A 530 TRP SER ASP ILE TRP ASN ALA THR LYS TYR ALA ASN SER
SEQRES 6 A 530 CYS CYS GLN ASN ILE ASP GLN SER PHE PRO GLY PHE HIS
SEQRES 7 A 530 GLY SER GLU MET TRP ASN PRO ASN THR ASP LEU SER GLU
SEQRES 8 A 530 ASP CYS LEU TYR LEU ASN VAL TRP ILE PRO ALA PRO LYS
SEQRES 9 A 530 PRO LYS ASN ALA THR VAL LEU ILE TRP ILE TYR GLY GLY
SEQRES 10 A 530 GLY PHE GLN THR GLY THR SER SER LEU HIS VAL TYR ASP
SEQRES 11 A 530 GLY LYS PHE LEU ALA ARG VAL GLU ARG VAL ILE VAL VAL
SEQRES 12 A 530 SER MET ASN TYR ARG VAL GLY ALA LEU GLY PHE LEU ALA
SEQRES 13 A 530 LEU PRO GLY ASN PRO GLU ALA PRO GLY ASN MET GLY LEU
SEQRES 14 A 530 PHE ASP GLN GLN LEU ALA LEU GLN TRP VAL GLN LYS ASN
SEQRES 15 A 530 ILE ALA ALA PHE GLY GLY ASN PRO LYS SER VAL THR LEU
SEQRES 16 A 530 PHE GLY GLU SER ALA GLY ALA ALA SER VAL SER LEU HIS
SEQRES 17 A 530 LEU LEU SER PRO GLY SER HIS SER LEU PHE THR ARG ALA
SEQRES 18 A 530 ILE LEU GLN SER GLY SER PHE ASN ALA PRO TRP ALA VAL
SEQRES 19 A 530 THR SER LEU TYR GLU ALA ARG ASN ARG THR LEU ASN LEU
SEQRES 20 A 530 ALA LYS LEU THR GLY CYS SER ARG GLU ASN GLU THR GLU
SEQRES 21 A 530 ILE ILE LYS CYS LEU ARG ASN LYS ASP PRO GLN GLU ILE
SEQRES 22 A 530 LEU LEU ASN GLU ALA PHE VAL VAL PRO TYR GLY THR PRO
SEQRES 23 A 530 LEU SER VAL ASN PHE GLY PRO THR VAL ASP GLY ASP PHE
SEQRES 24 A 530 LEU THR ASP MET PRO ASP ILE LEU LEU GLU LEU GLY GLN
SEQRES 25 A 530 PHE LYS LYS THR GLN ILE LEU VAL GLY VAL ASN LYS ASP
SEQRES 26 A 530 GLU GLY THR ALA PHE LEU VAL TYR GLY ALA PRO GLY PHE
SEQRES 27 A 530 SER LYS ASP ASN ASN SER ILE ILE THR ARG LYS GLU PHE
SEQRES 28 A 530 GLN GLU GLY LEU LYS ILE PHE PHE PRO GLY VAL SER GLU
SEQRES 29 A 530 PHE GLY LYS GLU SER ILE LEU PHE HIS TYR THR ASP TRP
SEQRES 30 A 530 VAL ASP ASP GLN ARG PRO GLU ASN TYR ARG GLU ALA LEU
SEQRES 31 A 530 GLY ASP VAL VAL GLY ASP TYR ASN PHE ILE CYS PRO ALA
SEQRES 32 A 530 LEU GLU PHE THR LYS LYS PHE SER GLU TRP GLY ASN ASN
SEQRES 33 A 530 ALA PHE PHE TYR TYR PHE GLU HIS ARG SER SER LYS LEU
SEQRES 34 A 530 PRO TRP PRO GLU TRP MET GLY VAL MET HIS GLY TYR GLU
SEQRES 35 A 530 ILE GLU PHE VAL PHE GLY LEU PRO LEU GLU ARG ARG ASP
SEQRES 36 A 530 ASN TYR THR LYS ALA GLU GLU ILE LEU SER ARG SER ILE
SEQRES 37 A 530 VAL LYS ARG TRP ALA ASN PHE ALA LYS TYR GLY ASN PRO
SEQRES 38 A 530 ASN GLU THR GLN ASN ASN SER THR SER TRP PRO VAL PHE
SEQRES 39 A 530 LYS SER THR GLU GLN LYS TYR LEU THR LEU ASN THR GLU
SEQRES 40 A 530 SER THR ARG ILE MET THR LYS LEU ARG ALA GLN GLN CYS
SEQRES 41 A 530 ARG PHE TRP THR SER PHE PHE PRO LYS VAL
SEQRES 1 B 530 THR GLU ASP ASP ILE ILE ILE ALA THR LYS ASN GLY LYS
SEQRES 2 B 530 VAL ARG GLY MET ASN LEU THR VAL PHE GLY GLY THR VAL
SEQRES 3 B 530 THR ALA PHE LEU GLY ILE PRO TYR ALA GLN PRO PRO LEU
SEQRES 4 B 530 GLY ARG LEU ARG PHE LYS LYS PRO GLN SER LEU THR LYS
SEQRES 5 B 530 TRP SER ASP ILE TRP ASN ALA THR LYS TYR ALA ASN SER
SEQRES 6 B 530 CYS CYS GLN ASN ILE ASP GLN SER PHE PRO GLY PHE HIS
SEQRES 7 B 530 GLY SER GLU MET TRP ASN PRO ASN THR ASP LEU SER GLU
SEQRES 8 B 530 ASP CYS LEU TYR LEU ASN VAL TRP ILE PRO ALA PRO LYS
SEQRES 9 B 530 PRO LYS ASN ALA THR VAL LEU ILE TRP ILE TYR GLY GLY
SEQRES 10 B 530 GLY PHE GLN THR GLY THR SER SER LEU HIS VAL TYR ASP
SEQRES 11 B 530 GLY LYS PHE LEU ALA ARG VAL GLU ARG VAL ILE VAL VAL
SEQRES 12 B 530 SER MET ASN TYR ARG VAL GLY ALA LEU GLY PHE LEU ALA
SEQRES 13 B 530 LEU PRO GLY ASN PRO GLU ALA PRO GLY ASN MET GLY LEU
SEQRES 14 B 530 PHE ASP GLN GLN LEU ALA LEU GLN TRP VAL GLN LYS ASN
SEQRES 15 B 530 ILE ALA ALA PHE GLY GLY ASN PRO LYS SER VAL THR LEU
SEQRES 16 B 530 PHE GLY GLU SER ALA GLY ALA ALA SER VAL SER LEU HIS
SEQRES 17 B 530 LEU LEU SER PRO GLY SER HIS SER LEU PHE THR ARG ALA
SEQRES 18 B 530 ILE LEU GLN SER GLY SER PHE ASN ALA PRO TRP ALA VAL
SEQRES 19 B 530 THR SER LEU TYR GLU ALA ARG ASN ARG THR LEU ASN LEU
SEQRES 20 B 530 ALA LYS LEU THR GLY CYS SER ARG GLU ASN GLU THR GLU
SEQRES 21 B 530 ILE ILE LYS CYS LEU ARG ASN LYS ASP PRO GLN GLU ILE
SEQRES 22 B 530 LEU LEU ASN GLU ALA PHE VAL VAL PRO TYR GLY THR PRO
SEQRES 23 B 530 LEU SER VAL ASN PHE GLY PRO THR VAL ASP GLY ASP PHE
SEQRES 24 B 530 LEU THR ASP MET PRO ASP ILE LEU LEU GLU LEU GLY GLN
SEQRES 25 B 530 PHE LYS LYS THR GLN ILE LEU VAL GLY VAL ASN LYS ASP
SEQRES 26 B 530 GLU GLY THR ALA PHE LEU VAL TYR GLY ALA PRO GLY PHE
SEQRES 27 B 530 SER LYS ASP ASN ASN SER ILE ILE THR ARG LYS GLU PHE
SEQRES 28 B 530 GLN GLU GLY LEU LYS ILE PHE PHE PRO GLY VAL SER GLU
SEQRES 29 B 530 PHE GLY LYS GLU SER ILE LEU PHE HIS TYR THR ASP TRP
SEQRES 30 B 530 VAL ASP ASP GLN ARG PRO GLU ASN TYR ARG GLU ALA LEU
SEQRES 31 B 530 GLY ASP VAL VAL GLY ASP TYR ASN PHE ILE CYS PRO ALA
SEQRES 32 B 530 LEU GLU PHE THR LYS LYS PHE SER GLU TRP GLY ASN ASN
SEQRES 33 B 530 ALA PHE PHE TYR TYR PHE GLU HIS ARG SER SER LYS LEU
SEQRES 34 B 530 PRO TRP PRO GLU TRP MET GLY VAL MET HIS GLY TYR GLU
SEQRES 35 B 530 ILE GLU PHE VAL PHE GLY LEU PRO LEU GLU ARG ARG ASP
SEQRES 36 B 530 ASN TYR THR LYS ALA GLU GLU ILE LEU SER ARG SER ILE
SEQRES 37 B 530 VAL LYS ARG TRP ALA ASN PHE ALA LYS TYR GLY ASN PRO
SEQRES 38 B 530 ASN GLU THR GLN ASN ASN SER THR SER TRP PRO VAL PHE
SEQRES 39 B 530 LYS SER THR GLU GLN LYS TYR LEU THR LEU ASN THR GLU
SEQRES 40 B 530 SER THR ARG ILE MET THR LYS LEU ARG ALA GLN GLN CYS
SEQRES 41 B 530 ARG PHE TRP THR SER PHE PHE PRO LYS VAL
HET 5HF A 601 32
HET GOL A 602 6
HET GOL A 603 6
HET GOL A 604 6
HET GOL A 605 6
HET EDO A 606 4
HET EDO A 607 4
HET EDO A 608 4
HET EDO A 609 4
HET EDO A 610 4
HET EDO A 611 4
HET CL A 612 1
HET CL A 613 1
HET PG4 A 614 13
HET NAG A 615 14
HET NAG A 616 14
HET NAG A 617 14
HET NAG A 618 14
HET FUC A 619 10
HET NAG A 620 14
HET NAG A 621 14
HET NAG A 622 14
HET NAG A 623 14
HET FUC A 624 10
HET NAG A 625 14
HET NAG A 626 14
HET NAG A 627 14
HET NAG A 628 14
HET NAG A 629 14
HET FUL A 630 10
HET 5HF B 601 32
HET GOL B 602 6
HET GOL B 603 6
HET GOL B 604 6
HET GOL B 605 6
HET GOL B 606 6
HET EDO B 607 4
HET EDO B 608 4
HET EDO B 609 4
HET CL B 610 1
HET CL B 611 1
HET NAG B 612 14
HET NAG B 613 14
HET NAG B 614 14
HET NAG B 615 14
HET NAG B 616 14
HET FUL B 617 10
HET NAG B 618 14
HET NAG B 619 14
HET FUL B 620 10
HET NAG B 621 14
HET NAG B 622 14
HET NAG B 623 14
HET FUL B 624 10
HET NAG B 625 14
HETNAM 5HF N-{[(3S)-1-BENZYLPIPERIDIN-3-YL]METHYL}-N-(2-
HETNAM 2 5HF METHOXYETHYL)NAPHTHALENE-2-SULFONAMIDE
HETNAM GOL GLYCEROL
HETNAM EDO 1,2-ETHANEDIOL
HETNAM CL CHLORIDE ION
HETNAM PG4 TETRAETHYLENE GLYCOL
HETNAM NAG N-ACETYL-D-GLUCOSAMINE
HETNAM FUC ALPHA-L-FUCOSE
HETNAM FUL BETA-L-FUCOSE
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
HETSYN EDO ETHYLENE GLYCOL
HETSYN FUL 6-DEOXY-BETA-L-GALACTOSE
FORMUL 3 5HF 2(C26 H32 N2 O3 S)
FORMUL 4 GOL 9(C3 H8 O3)
FORMUL 8 EDO 9(C2 H6 O2)
FORMUL 14 CL 4(CL 1-)
FORMUL 16 PG4 C8 H18 O5
FORMUL 17 NAG 24(C8 H15 N O6)
FORMUL 18 FUC 2(C6 H12 O5)
FORMUL 23 FUL 4(C6 H12 O5)
FORMUL 43 HOH *285(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 VAL A 148 LEU A 154 1 7
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 PRO A 211 PHE A 217 5 7
HELIX 10 AB1 SER A 235 THR A 250 1 16
HELIX 11 AB2 ASN A 256 LYS A 267 1 12
HELIX 12 AB3 ASP A 268 LEU A 274 1 7
HELIX 13 AB4 ASN A 275 VAL A 279 5 5
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 279 5 5
HELIX 39 AE3 MET B 302 LEU B 309 1 8
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 GLU B 451 5 5
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 TRP A 56 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 GLY A 23 N VAL A 20
SHEET 3 AA211 TYR A 94 PRO A 100 -1 O ILE A 99 N THR A 26
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 TRP A 112 O VAL A 142
SHEET 6 AA211 GLY A 187 GLU A 197 1 O SER A 191 N VAL A 109
SHEET 7 AA211 ARG A 219 GLN A 223 1 O ARG A 219 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 501 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 ARG B 14
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 PRO B 100 -1 O ILE B 99 N THR B 26
SHEET 4 AA411 ILE B 140 MET B 144 -1 O VAL B 141 N TRP B 98
SHEET 5 AA411 ALA B 107 ILE B 113 1 N LEU B 110 O ILE B 140
SHEET 6 AA411 GLY B 187 GLU B 197 1 O ASN B 188 N ALA B 107
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 2.06
SSBOND 2 CYS A 252 CYS A 263 1555 1555 2.05
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 615 1555 1555 1.45
LINK ND2 ASN A 57 C1 NAG A 617 1555 1555 1.44
LINK ND2 ASN A 106 C1 NAG A 620 1555 1555 1.41
LINK ND2 ASN A 241 C1 NAG A 622 1555 1555 1.43
LINK ND2 ASN A 341 C1 NAG A 625 1555 1555 1.50
LINK ND2 ASN A 481 C1 NAG A 626 1555 1555 1.50
LINK ND2 ASN A 486 C1 NAG A 628 1555 1555 1.47
LINK ND2 ASN B 17 C1 NAG B 612 1555 1555 1.50
LINK ND2 ASN B 57 C1 NAG B 613 1555 1555 1.54
LINK ND2 ASN B 106 C1 NAG B 614 1555 1555 1.46
LINK ND2 ASN B 241 C1 NAG B 615 1555 1555 1.48
LINK ND2 ASN B 256 C1 NAG B 618 1555 1555 1.31
LINK ND2 ASN B 341 C1 NAG B 621 1555 1555 1.50
LINK ND2 ASN B 455 C1 NAG B 622 1555 1555 1.46
LINK ND2 ASN B 481 C1 NAG B 625 1555 1555 1.49
LINK O4 NAG A 615 C1 NAG A 616 1555 1555 1.46
LINK O4 NAG A 617 C1 NAG A 618 1555 1555 1.45
LINK O6 NAG A 617 C1 FUC A 619 1555 1555 1.44
LINK O4 NAG A 620 C1 NAG A 621 1555 1555 1.54
LINK O4 NAG A 622 C1 NAG A 623 1555 1555 1.46
LINK O6 NAG A 622 C1 FUC A 624 1555 1555 1.49
LINK O4 NAG A 626 C1 NAG A 627 1555 1555 1.49
LINK O4 NAG A 628 C1 NAG A 629 1555 1555 1.49
LINK O6 NAG A 628 C1 FUL A 630 1555 1555 1.44
LINK O4 NAG B 615 C1 NAG B 616 1555 1555 1.55
LINK O6 NAG B 615 C1 FUL B 617 1555 1555 1.51
LINK O4 NAG B 618 C1 NAG B 619 1555 1555 1.42
LINK O6 NAG B 618 C1 FUL B 620 1555 1555 1.47
LINK O4 NAG B 622 C1 NAG B 623 1555 1555 1.43
LINK O6 NAG B 622 C1 FUL B 624 1555 1555 1.47
CISPEP 1 ALA A 101 PRO A 102 0 -1.62
CISPEP 2 GLN A 380 ARG A 381 0 -6.63
CISPEP 3 ALA B 101 PRO B 102 0 0.93
SITE 1 AC1 12 ASN A 68 GLY A 116 GLY A 117 GLN A 119
SITE 2 AC1 12 THR A 120 SER A 198 TRP A 231 SER A 287
SITE 3 AC1 12 PHE A 398 TRP A 430 MET A 437 HIS A 438
SITE 1 AC2 5 LEU A 18 TYR A 61 TRP A 98 ASP A 129
SITE 2 AC2 5 LYS A 131
SITE 1 AC3 6 PRO A 189 LYS A 190 SER A 215 PHE A 217
SITE 2 AC3 6 THR A 218 LYS A 313
SITE 1 AC4 5 TYR A 396 CYS A 400 PRO A 401 TRP A 522
SITE 2 AC4 5 THR A 523
SITE 1 AC5 5 TYR A 33 SER A 48 LEU A 49 TRP A 177
SITE 2 AC5 5 LYS A 180
SITE 1 AC6 4 ASN A 479 TRP A 490 HOH A 759 GLN B 71
SITE 1 AC7 2 THR A 108 ASN A 188
SITE 1 AC8 3 HIS A 77 LYS A 427 GLU A 443
SITE 1 AC9 3 LYS A 494 SER A 495 THR A 496
SITE 1 AD1 3 ARG A 386 GLU A 387 TRP A 433
SITE 1 AD2 8 LEU A 29 GLY A 30 TRP A 56 ASN A 57
SITE 2 AD2 8 LYS A 60 ALA A 62 TYR A 94 HOH A 777
SITE 1 AD3 1 ARG A 386
SITE 1 AD4 1 GLU A 197
SITE 1 AD5 4 SER A 426 ASN A 455 TYR A 456 NAG A 616
SITE 1 AD6 16 ASN B 68 ILE B 69 ASP B 70 TRP B 82
SITE 2 AD6 16 GLY B 116 GLY B 117 GLN B 119 THR B 120
SITE 3 AD6 16 SER B 198 SER B 287 ALA B 328 PHE B 329
SITE 4 AD6 16 PHE B 398 TRP B 430 MET B 437 HIS B 438
SITE 1 AD7 5 LEU B 18 TYR B 61 TRP B 98 ASP B 129
SITE 2 AD7 5 LYS B 131
SITE 1 AD8 6 ARG B 240 LEU B 244 GLU B 255 GLU B 411
SITE 2 AD8 6 TRP B 412 GLY B 413
SITE 1 AD9 3 PRO B 46 GLN B 47 SER B 48
SITE 1 AE1 5 TRP B 231 THR B 284 LEU B 286 SER B 287
SITE 2 AE1 5 ASN B 397
SITE 1 AE2 7 PRO B 449 GLU B 451 ARG B 452 ASP B 454
SITE 2 AE2 7 ASN B 455 TYR B 456 GLU B 461
SITE 1 AE3 2 ARG B 42 LYS B 267
SITE 1 AE4 4 LYS A 528 ARG B 347 GLN B 351 GLU B 367
SITE 1 AE5 2 HIS B 77 GLU B 443
SITE 1 AE6 2 ARG B 242 VAL B 288
SITE 1 AE7 1 GLU B 197
SITE 1 AE8 4 ASN A 17 THR A 24 PG4 A 614 HOH A 764
SITE 1 AE9 4 ARG A 14 ILE A 55 ASN A 57 LYS B 12
SITE 1 AF1 3 ASN A 106 ASN A 188 LYS A 190
SITE 1 AF2 9 ASN A 241 ASN A 245 LYS A 248 PHE A 278
SITE 2 AF2 9 VAL A 280 PRO A 281 NAG B 622 NAG B 623
SITE 3 AF2 9 FUL B 624
SITE 1 AF3 5 SER A 338 ASN A 341 HOH A 702 HOH A 727
SITE 2 AF3 5 HOH A 799
SITE 1 AF4 9 TYR A 477 ASN A 479 ASN A 481 GLU A 482
SITE 2 AF4 9 THR A 483 GLN A 484 ASP B 87 LEU B 88
SITE 3 AF4 9 GLN B 270
SITE 1 AF5 6 GLU A 482 ASN A 486 SER A 487 THR A 488
SITE 2 AF5 6 THR A 508 GLY B 75
SITE 1 AF6 2 ASN B 17 HOH B 703
SITE 1 AF7 3 ARG B 14 ASN B 57 HOH B 783
SITE 1 AF8 2 ASN B 106 ASN B 188
SITE 1 AF9 8 TYR B 237 ASN B 241 ASN B 245 PHE B 278
SITE 2 AF9 8 VAL B 280 PRO B 281 TYR B 282 GLN B 380
SITE 1 AG1 2 GLU B 255 ASN B 256
SITE 1 AG2 3 SER B 338 ASN B 341 HOH B 735
SITE 1 AG3 7 ARG A 240 ASN A 241 LEU A 244 NAG A 622
SITE 2 AG3 7 LYS B 427 ASP B 454 ASN B 455
SITE 1 AG4 4 ILE B 305 TYR B 477 ASN B 481 GLU B 482
CRYST1 72.214 78.863 226.650 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 0.013848 0.000000 0.000000 0.00000
SCALE2 0.000000 0.012680 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004412 0.00000
TER 4213 VAL A 529
TER 8384 VAL B 529
MASTER 510 0 55 50 28 0 62 6 9211 2 590 82
END |