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HEADER HYDROLASE 11-DEC-17 6F7Q
TITLE HUMAN BUTYRYLCHOLINESTERASE COMPLEXED WITH N-PROPARGYLIPERIDINES
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_TAXID: 10029
KEYWDS ALZHEIMER DISEASE AD BUTYRYLCHOLINESTERASE N-PROPARGYLIPERIDINES,
KEYWDS 2 HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR N.COQUELLE,D.KNEZ,J.P.COLLETIER,S.GOBEC
REVDAT 1 05-SEP-18 6F7Q 0
JRNL AUTH D.KNEZ,N.COQUELLE,A.PISLAR,S.ZAKELJ,M.JUKIC,M.SOVA,
JRNL AUTH 2 J.MRAVLJAK,F.NACHON,X.BRAZZOLOTTO,J.KOS,J.P.COLLETIER,
JRNL AUTH 3 S.GOBEC
JRNL TITL MULTI-TARGET-DIRECTED LIGANDS FOR TREATING ALZHEIMER'S
JRNL TITL 2 DISEASE: BUTYRYLCHOLINESTERASE INHIBITORS DISPLAYING
JRNL TITL 3 ANTIOXIDANT AND NEUROPROTECTIVE ACTIVITIES.
JRNL REF EUR.J.MED.CHEM. V. 156 598 2018
JRNL REFN ISSN 0223-5234
JRNL PMID 30031971
JRNL DOI 10.1016/J.EJMECH.2018.07.033
REMARK 2
REMARK 2 RESOLUTION. 2.60 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (1.11.1_2575: ???)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.60
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 49.11
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 94.1
REMARK 3 NUMBER OF REFLECTIONS : 48664
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.194
REMARK 3 R VALUE (WORKING SET) : 0.192
REMARK 3 FREE R VALUE : 0.248
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 2434
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 49.1181 - 6.6801 0.92 2897 154 0.1798 0.2613
REMARK 3 2 6.6801 - 5.3042 0.95 2816 147 0.1780 0.2181
REMARK 3 3 5.3042 - 4.6343 0.95 2794 147 0.1418 0.1807
REMARK 3 4 4.6343 - 4.2109 0.95 2787 147 0.1339 0.1789
REMARK 3 5 4.2109 - 3.9092 0.95 2743 145 0.1523 0.1879
REMARK 3 6 3.9092 - 3.6788 0.92 2677 141 0.1705 0.2100
REMARK 3 7 3.6788 - 3.4946 0.94 2704 142 0.1890 0.2694
REMARK 3 8 3.4946 - 3.3425 0.94 2685 141 0.2096 0.2867
REMARK 3 9 3.3425 - 3.2139 0.94 2703 142 0.2192 0.2698
REMARK 3 10 3.2139 - 3.1030 0.94 2657 140 0.2531 0.3364
REMARK 3 11 3.1030 - 3.0060 0.94 2705 143 0.2541 0.3495
REMARK 3 12 3.0060 - 2.9200 0.94 2677 141 0.2674 0.3300
REMARK 3 13 2.9200 - 2.8432 0.94 2688 141 0.2741 0.3052
REMARK 3 14 2.8432 - 2.7738 0.94 2673 141 0.2891 0.3727
REMARK 3 15 2.7738 - 2.7108 0.93 2647 139 0.3092 0.4081
REMARK 3 16 2.7108 - 2.6531 0.94 2695 142 0.3256 0.3735
REMARK 3 17 2.6531 - 2.6000 0.95 2682 141 0.3208 0.3753
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) : 0.430
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 27.760
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 : 0.009 9090
REMARK 3 ANGLE : 1.019 12346
REMARK 3 CHIRALITY : 0.060 1338
REMARK 3 PLANARITY : 0.006 1550
REMARK 3 DIHEDRAL : 19.118 5371
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 6F7Q COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 12-DEC-17.
REMARK 100 THE DEPOSITION ID IS D_1200007731.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 06-NOV-15
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.9
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : MASSIF-3
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9679
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 : 49669
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.600
REMARK 200 RESOLUTION RANGE LOW (A) : 49.109
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 94.0
REMARK 200 DATA REDUNDANCY : 2.800
REMARK 200 R MERGE (I) : 0.09710
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 7.0400
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.60
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.69
REMARK 200 COMPLETENESS FOR SHELL (%) : 94.8
REMARK 200 DATA REDUNDANCY IN SHELL : 2.70
REMARK 200 R MERGE FOR SHELL (I) : 0.96110
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 (%): 64.38
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.45
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M TRIS, 2.3 M AMMONIUM SULFATE, PH
REMARK 280 8.9, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 4 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z
REMARK 290 3555 -Y+1/2,X+1/2,Z
REMARK 290 4555 Y+1/2,-X+1/2,Z
REMARK 290 5555 -X+1/2,Y+1/2,-Z
REMARK 290 6555 X+1/2,-Y+1/2,-Z
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -Y,-X,-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 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 76.07000
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 76.07000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 76.07000
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 76.07000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 76.07000
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 76.07000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 76.07000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 76.07000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 9580 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 40360 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 6.0 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 GLU A 1
REMARK 465 ASP A 2
REMARK 465 GLU B 1
REMARK 465 ASP B 2
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 ARG A 40 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 51 CG CD CE NZ
REMARK 470 SER A 53 OG
REMARK 470 TYR A 237 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 ARG A 240 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 248 CG CD CE NZ
REMARK 470 TYR A 282 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 ARG A 452 CG CD NE CZ NH1 NH2
REMARK 470 ARG A 520 CG CD NE CZ NH1 NH2
REMARK 470 LYS B 12 CG CD CE NZ
REMARK 470 LYS B 51 CG CD CE NZ
REMARK 470 SER B 53 OG
REMARK 470 ARG B 240 CG CD NE CZ NH1 NH2
REMARK 470 TYR B 282 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 GLN B 380 CG CD OE1 NE2
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 CG ASN A 341 C1 NAG A 616 1.76
REMARK 500 O4 NAG B 608 O5 NAG B 609 1.81
REMARK 500 ND2 ASN A 485 C2 NAG A 615 2.09
REMARK 500 ND2 ASN A 57 C2 NAG A 609 2.13
REMARK 500 OD2 ASP A 87 O HOH A 701 2.14
REMARK 500 O6 NAG B 608 O5 FUC B 610 2.17
REMARK 500 CG ASN B 341 C1 NAG B 608 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 MET A 16 138.16 -171.27
REMARK 500 PHE A 153 10.33 -145.62
REMARK 500 ALA A 162 70.83 -151.95
REMARK 500 SER A 198 -120.90 53.78
REMARK 500 CYS A 252 49.68 -165.28
REMARK 500 PRO A 281 -86.70 -60.46
REMARK 500 ASP A 297 -74.74 -133.17
REMARK 500 ILE A 344 105.38 -56.21
REMARK 500 ASP A 375 32.29 -79.53
REMARK 500 GLN A 380 37.22 -89.05
REMARK 500 PHE A 398 -52.23 -130.93
REMARK 500 TRP A 412 32.16 -99.82
REMARK 500 GLU A 451 92.51 -66.15
REMARK 500 ARG A 453 34.55 -82.14
REMARK 500 PRO A 480 44.61 -94.61
REMARK 500 ASN A 485 44.60 -100.47
REMARK 500 LYS A 513 71.11 62.59
REMARK 500 LYS B 9 -6.59 -59.35
REMARK 500 ASN B 10 25.73 -140.39
REMARK 500 SER B 48 171.80 -46.20
REMARK 500 SER B 53 38.25 -91.55
REMARK 500 ILE B 55 126.08 41.44
REMARK 500 GLN B 67 141.61 -170.81
REMARK 500 THR B 86 -165.87 -128.21
REMARK 500 SER B 89 147.68 -172.79
REMARK 500 PHE B 118 11.17 57.65
REMARK 500 PRO B 160 1.23 -69.81
REMARK 500 ALA B 162 82.73 -150.00
REMARK 500 SER B 198 -118.39 51.21
REMARK 500 SER B 253 73.69 -63.50
REMARK 500 ARG B 254 -163.82 -76.39
REMARK 500 GLU B 255 -21.95 -141.36
REMARK 500 PRO B 281 -81.90 -54.70
REMARK 500 ASP B 297 -73.91 -128.85
REMARK 500 THR B 315 -179.18 -170.27
REMARK 500 TYR B 332 45.32 -105.19
REMARK 500 PHE B 358 73.20 -114.10
REMARK 500 ASP B 375 44.08 -84.14
REMARK 500 GLN B 380 47.03 -79.64
REMARK 500 PHE B 398 -59.20 -135.49
REMARK 500 ARG B 453 31.05 -75.88
REMARK 500 PRO B 480 45.18 -88.44
REMARK 500 GLN B 484 -30.70 -130.16
REMARK 500 ASN B 485 45.70 -102.91
REMARK 500 ASN B 504 -178.27 -172.87
REMARK 500 GLU B 506 -80.34 -92.74
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CWQ A 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CWQ 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 SO4 A 619
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 620
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 621
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CWQ B 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CWQ B 602
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL B 603
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 604
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue NAG B 605
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 615
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 616
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG A
REMARK 800 609 through FUL A 610 bound to ASN A 57
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG A 611 bound
REMARK 800 to ASN A 106
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG A
REMARK 800 612 through NAG A 614 bound to ASN A 241
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG A
REMARK 800 616 through NAG A 618 bound to ASN A 341
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG A 615 bound
REMARK 800 to ASN A 485
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG B
REMARK 800 606 through NAG B 607 bound to ASN B 106
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG B
REMARK 800 612 through NAG B 614 bound to ASN B 241
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG B
REMARK 800 608 through FUC B 610 bound to ASN B 341
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG B 611 bound
REMARK 800 to ASN B 485
DBREF 6F7Q A 1 529 UNP P06276 CHLE_HUMAN 29 557
DBREF 6F7Q B 1 529 UNP P06276 CHLE_HUMAN 29 557
SEQRES 1 A 529 GLU ASP ASP ILE ILE ILE ALA THR LYS ASN GLY LYS VAL
SEQRES 2 A 529 ARG GLY MET ASN LEU THR VAL PHE GLY GLY THR VAL THR
SEQRES 3 A 529 ALA PHE LEU GLY ILE PRO TYR ALA GLN PRO PRO LEU GLY
SEQRES 4 A 529 ARG LEU ARG PHE LYS LYS PRO GLN SER LEU THR LYS TRP
SEQRES 5 A 529 SER ASP ILE TRP ASN ALA THR LYS TYR ALA ASN SER CYS
SEQRES 6 A 529 CYS GLN ASN ILE ASP GLN SER PHE PRO GLY PHE HIS GLY
SEQRES 7 A 529 SER GLU MET TRP ASN PRO ASN THR ASP LEU SER GLU ASP
SEQRES 8 A 529 CYS LEU TYR LEU ASN VAL TRP ILE PRO ALA PRO LYS PRO
SEQRES 9 A 529 LYS ASN ALA THR VAL LEU ILE TRP ILE TYR GLY GLY GLY
SEQRES 10 A 529 PHE GLN THR GLY THR SER SER LEU HIS VAL TYR ASP GLY
SEQRES 11 A 529 LYS PHE LEU ALA ARG VAL GLU ARG VAL ILE VAL VAL SER
SEQRES 12 A 529 MET ASN TYR ARG VAL GLY ALA LEU GLY PHE LEU ALA LEU
SEQRES 13 A 529 PRO GLY ASN PRO GLU ALA PRO GLY ASN MET GLY LEU PHE
SEQRES 14 A 529 ASP GLN GLN LEU ALA LEU GLN TRP VAL GLN LYS ASN ILE
SEQRES 15 A 529 ALA ALA PHE GLY GLY ASN PRO LYS SER VAL THR LEU PHE
SEQRES 16 A 529 GLY GLU SER ALA GLY ALA ALA SER VAL SER LEU HIS LEU
SEQRES 17 A 529 LEU SER PRO GLY SER HIS SER LEU PHE THR ARG ALA ILE
SEQRES 18 A 529 LEU GLN SER GLY SER PHE ASN ALA PRO TRP ALA VAL THR
SEQRES 19 A 529 SER LEU TYR GLU ALA ARG ASN ARG THR LEU ASN LEU ALA
SEQRES 20 A 529 LYS LEU THR GLY CYS SER ARG GLU ASN GLU THR GLU ILE
SEQRES 21 A 529 ILE LYS CYS LEU ARG ASN LYS ASP PRO GLN GLU ILE LEU
SEQRES 22 A 529 LEU ASN GLU ALA PHE VAL VAL PRO TYR GLY THR PRO LEU
SEQRES 23 A 529 SER VAL ASN PHE GLY PRO THR VAL ASP GLY ASP PHE LEU
SEQRES 24 A 529 THR ASP MET PRO ASP ILE LEU LEU GLU LEU GLY GLN PHE
SEQRES 25 A 529 LYS LYS THR GLN ILE LEU VAL GLY VAL ASN LYS ASP GLU
SEQRES 26 A 529 GLY THR ALA PHE LEU VAL TYR GLY ALA PRO GLY PHE SER
SEQRES 27 A 529 LYS ASP ASN ASN SER ILE ILE THR ARG LYS GLU PHE GLN
SEQRES 28 A 529 GLU GLY LEU LYS ILE PHE PHE PRO GLY VAL SER GLU PHE
SEQRES 29 A 529 GLY LYS GLU SER ILE LEU PHE HIS TYR THR ASP TRP VAL
SEQRES 30 A 529 ASP ASP GLN ARG PRO GLU ASN TYR ARG GLU ALA LEU GLY
SEQRES 31 A 529 ASP VAL VAL GLY ASP TYR ASN PHE ILE CYS PRO ALA LEU
SEQRES 32 A 529 GLU PHE THR LYS LYS PHE SER GLU TRP GLY ASN ASN ALA
SEQRES 33 A 529 PHE PHE TYR TYR PHE GLU HIS ARG SER SER LYS LEU PRO
SEQRES 34 A 529 TRP PRO GLU TRP MET GLY VAL MET HIS GLY TYR GLU ILE
SEQRES 35 A 529 GLU PHE VAL PHE GLY LEU PRO LEU GLU ARG ARG ASP ASN
SEQRES 36 A 529 TYR THR LYS ALA GLU GLU ILE LEU SER ARG SER ILE VAL
SEQRES 37 A 529 LYS ARG TRP ALA ASN PHE ALA LYS TYR GLY ASN PRO ASN
SEQRES 38 A 529 GLU THR GLN ASN ASN SER THR SER TRP PRO VAL PHE LYS
SEQRES 39 A 529 SER THR GLU GLN LYS TYR LEU THR LEU ASN THR GLU SER
SEQRES 40 A 529 THR ARG ILE MET THR LYS LEU ARG ALA GLN GLN CYS ARG
SEQRES 41 A 529 PHE TRP THR SER PHE PHE PRO LYS VAL
SEQRES 1 B 529 GLU ASP ASP ILE ILE ILE ALA THR LYS ASN GLY LYS VAL
SEQRES 2 B 529 ARG GLY MET ASN LEU THR VAL PHE GLY GLY THR VAL THR
SEQRES 3 B 529 ALA PHE LEU GLY ILE PRO TYR ALA GLN PRO PRO LEU GLY
SEQRES 4 B 529 ARG LEU ARG PHE LYS LYS PRO GLN SER LEU THR LYS TRP
SEQRES 5 B 529 SER ASP ILE TRP ASN ALA THR LYS TYR ALA ASN SER CYS
SEQRES 6 B 529 CYS GLN ASN ILE ASP GLN SER PHE PRO GLY PHE HIS GLY
SEQRES 7 B 529 SER GLU MET TRP ASN PRO ASN THR ASP LEU SER GLU ASP
SEQRES 8 B 529 CYS LEU TYR LEU ASN VAL TRP ILE PRO ALA PRO LYS PRO
SEQRES 9 B 529 LYS ASN ALA THR VAL LEU ILE TRP ILE TYR GLY GLY GLY
SEQRES 10 B 529 PHE GLN THR GLY THR SER SER LEU HIS VAL TYR ASP GLY
SEQRES 11 B 529 LYS PHE LEU ALA ARG VAL GLU ARG VAL ILE VAL VAL SER
SEQRES 12 B 529 MET ASN TYR ARG VAL GLY ALA LEU GLY PHE LEU ALA LEU
SEQRES 13 B 529 PRO GLY ASN PRO GLU ALA PRO GLY ASN MET GLY LEU PHE
SEQRES 14 B 529 ASP GLN GLN LEU ALA LEU GLN TRP VAL GLN LYS ASN ILE
SEQRES 15 B 529 ALA ALA PHE GLY GLY ASN PRO LYS SER VAL THR LEU PHE
SEQRES 16 B 529 GLY GLU SER ALA GLY ALA ALA SER VAL SER LEU HIS LEU
SEQRES 17 B 529 LEU SER PRO GLY SER HIS SER LEU PHE THR ARG ALA ILE
SEQRES 18 B 529 LEU GLN SER GLY SER PHE ASN ALA PRO TRP ALA VAL THR
SEQRES 19 B 529 SER LEU TYR GLU ALA ARG ASN ARG THR LEU ASN LEU ALA
SEQRES 20 B 529 LYS LEU THR GLY CYS SER ARG GLU ASN GLU THR GLU ILE
SEQRES 21 B 529 ILE LYS CYS LEU ARG ASN LYS ASP PRO GLN GLU ILE LEU
SEQRES 22 B 529 LEU ASN GLU ALA PHE VAL VAL PRO TYR GLY THR PRO LEU
SEQRES 23 B 529 SER VAL ASN PHE GLY PRO THR VAL ASP GLY ASP PHE LEU
SEQRES 24 B 529 THR ASP MET PRO ASP ILE LEU LEU GLU LEU GLY GLN PHE
SEQRES 25 B 529 LYS LYS THR GLN ILE LEU VAL GLY VAL ASN LYS ASP GLU
SEQRES 26 B 529 GLY THR ALA PHE LEU VAL TYR GLY ALA PRO GLY PHE SER
SEQRES 27 B 529 LYS ASP ASN ASN SER ILE ILE THR ARG LYS GLU PHE GLN
SEQRES 28 B 529 GLU GLY LEU LYS ILE PHE PHE PRO GLY VAL SER GLU PHE
SEQRES 29 B 529 GLY LYS GLU SER ILE LEU PHE HIS TYR THR ASP TRP VAL
SEQRES 30 B 529 ASP ASP GLN ARG PRO GLU ASN TYR ARG GLU ALA LEU GLY
SEQRES 31 B 529 ASP VAL VAL GLY ASP TYR ASN PHE ILE CYS PRO ALA LEU
SEQRES 32 B 529 GLU PHE THR LYS LYS PHE SER GLU TRP GLY ASN ASN ALA
SEQRES 33 B 529 PHE PHE TYR TYR PHE GLU HIS ARG SER SER LYS LEU PRO
SEQRES 34 B 529 TRP PRO GLU TRP MET GLY VAL MET HIS GLY TYR GLU ILE
SEQRES 35 B 529 GLU PHE VAL PHE GLY LEU PRO LEU GLU ARG ARG ASP ASN
SEQRES 36 B 529 TYR THR LYS ALA GLU GLU ILE LEU SER ARG SER ILE VAL
SEQRES 37 B 529 LYS ARG TRP ALA ASN PHE ALA LYS TYR GLY ASN PRO ASN
SEQRES 38 B 529 GLU THR GLN ASN ASN SER THR SER TRP PRO VAL PHE LYS
SEQRES 39 B 529 SER THR GLU GLN LYS TYR LEU THR LEU ASN THR GLU SER
SEQRES 40 B 529 THR ARG ILE MET THR LYS LEU ARG ALA GLN GLN CYS ARG
SEQRES 41 B 529 PHE TRP THR SER PHE PHE PRO LYS VAL
HET CWQ A 601 35
HET CWQ A 602 35
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 NAG A 609 14
HET FUL A 610 10
HET NAG A 611 14
HET NAG A 612 14
HET FUL A 613 10
HET NAG A 614 14
HET NAG A 615 14
HET NAG A 616 14
HET FUL A 617 10
HET NAG A 618 14
HET SO4 A 619 5
HET SO4 A 620 5
HET SO4 A 621 5
HET CWQ B 601 35
HET CWQ B 602 35
HET CL B 603 1
HET EDO B 604 4
HET NAG B 605 14
HET NAG B 606 14
HET NAG B 607 14
HET NAG B 608 14
HET NAG B 609 14
HET FUC B 610 10
HET NAG B 611 14
HET NAG B 612 14
HET FUL B 613 10
HET NAG B 614 14
HET SO4 B 615 5
HET SO4 B 616 5
HETNAM CWQ 2-[[(3~{R})-1-(2,3-DIHYDRO-1~{H}-INDEN-2-YL)PIPERIDIN-
HETNAM 2 CWQ 3-YL]METHYL-(8-OXIDANYLQUINOLIN-2-YL)CARBONYL-
HETNAM 3 CWQ AMINO]ETHYL-DIMETHYL-AZANIUM
HETNAM GOL GLYCEROL
HETNAM EDO 1,2-ETHANEDIOL
HETNAM NAG N-ACETYL-D-GLUCOSAMINE
HETNAM FUL BETA-L-FUCOSE
HETNAM SO4 SULFATE ION
HETNAM CL CHLORIDE ION
HETNAM FUC ALPHA-L-FUCOSE
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
HETSYN EDO ETHYLENE GLYCOL
HETSYN FUL 6-DEOXY-BETA-L-GALACTOSE
FORMUL 3 CWQ 4(C29 H37 N4 O2 1+)
FORMUL 5 GOL 3(C3 H8 O3)
FORMUL 8 EDO 4(C2 H6 O2)
FORMUL 11 NAG 15(C8 H15 N O6)
FORMUL 11 FUL 4(C6 H12 O5)
FORMUL 16 SO4 5(O4 S 2-)
FORMUL 21 CL CL 1-
FORMUL 25 FUC C6 H12 O5
FORMUL 30 HOH *123(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 GLU A 137 1 8
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 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 ARG A 265 1 10
HELIX 12 AB3 ASP A 268 GLU A 276 1 9
HELIX 13 AB4 ALA A 277 VAL A 280 5 4
HELIX 14 AB5 MET A 302 LEU A 309 1 8
HELIX 15 AB6 GLY A 326 LEU A 330 5 5
HELIX 16 AB7 THR A 346 PHE A 358 1 13
HELIX 17 AB8 SER A 362 THR A 374 1 13
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 VAL B 148 LEU B 154 1 7
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 SER B 210 SER B 215 1 6
HELIX 35 AD8 SER B 235 LEU B 249 1 15
HELIX 36 AD9 ASN B 256 LYS B 267 1 12
HELIX 37 AE1 ASP B 268 GLU B 276 1 9
HELIX 38 AE2 ALA B 277 VAL B 280 5 4
HELIX 39 AE3 MET B 302 LEU B 309 1 8
HELIX 40 AE4 GLY B 326 GLY B 333 5 8
HELIX 41 AE5 THR B 346 PHE B 358 1 13
HELIX 42 AE6 SER B 362 THR B 374 1 13
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 SER B 524 1 10
HELIX 50 AF5 PHE B 525 VAL B 529 5 5
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 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 PHE A 418
SHEET 11 AA211 ILE A 510 THR A 512 -1 O MET A 511 N TYR A 500
SHEET 1 AA3 3 ILE B 4 THR B 8 0
SHEET 2 AA3 3 GLY B 11 VAL B 20 -1 O GLY B 11 N THR B 8
SHEET 3 AA3 3 TRP B 52 ALA B 58 1 O TRP B 56 N ARG B 14
SHEET 1 AA412 ILE B 4 THR B 8 0
SHEET 2 AA412 GLY B 11 VAL B 20 -1 O GLY B 11 N THR B 8
SHEET 3 AA412 GLY B 23 PRO B 32 -1 O VAL B 25 N LEU B 18
SHEET 4 AA412 TYR B 94 PRO B 100 -1 O ILE B 99 N THR B 26
SHEET 5 AA412 ILE B 140 MET B 144 -1 O SER B 143 N ASN B 96
SHEET 6 AA412 ALA B 107 ILE B 113 1 N LEU B 110 O ILE B 140
SHEET 7 AA412 GLY B 187 GLU B 197 1 O ASN B 188 N ALA B 107
SHEET 8 AA412 ARG B 219 GLN B 223 1 O GLN B 223 N GLY B 196
SHEET 9 AA412 ILE B 317 ASN B 322 1 O LEU B 318 N LEU B 222
SHEET 10 AA412 ALA B 416 PHE B 421 1 O PHE B 417 N VAL B 319
SHEET 11 AA412 LYS B 499 LEU B 503 1 O LEU B 503 N TYR B 420
SHEET 12 AA412 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 2.02
SSBOND 3 CYS A 400 CYS A 519 1555 1555 2.04
SSBOND 4 CYS B 65 CYS B 92 1555 1555 2.03
SSBOND 5 CYS B 252 CYS B 263 1555 1555 2.04
SSBOND 6 CYS B 400 CYS B 519 1555 1555 2.06
LINK ND2 ASN A 57 C1 NAG A 609 1555 1555 1.47
LINK ND2 ASN A 106 C1 NAG A 611 1555 1555 1.49
LINK ND2 ASN A 241 C1 NAG A 612 1555 1555 1.47
LINK ND2 ASN A 341 C1 NAG A 616 1555 1555 1.25
LINK ND2 ASN A 341 O5 NAG A 616 1555 1555 1.31
LINK ND2 ASN A 485 C1 NAG A 615 1555 1555 1.50
LINK ND2 ASN B 106 C1 NAG B 606 1555 1555 1.50
LINK ND2 ASN B 241 C1 NAG B 612 1555 1555 1.46
LINK ND2 ASN B 341 C1 NAG B 608 1555 1555 1.42
LINK ND2 ASN B 485 C1 NAG B 611 1555 1555 1.52
LINK O6 NAG A 609 C1 FUL A 610 1555 1555 1.37
LINK O4 NAG A 612 C1 NAG A 614 1555 1555 1.45
LINK O6 NAG A 612 C1 FUL A 613 1555 1555 1.45
LINK O4 NAG A 616 C1 NAG A 618 1555 1555 1.44
LINK O6 NAG A 616 C1 FUL A 617 1555 1555 1.44
LINK O4 NAG B 606 C1 NAG B 607 1555 1555 1.41
LINK O4 NAG B 608 C1 NAG B 609 1555 1555 1.48
LINK O6 NAG B 608 C1 FUC B 610 1555 1555 1.44
LINK O4 NAG B 612 C1 NAG B 614 1555 1555 1.45
LINK O6 NAG B 612 C1 FUL B 613 1555 1555 1.45
LINK ND2 ASN B 57 C1 NAG B 605 1555 1555 1.86
CISPEP 1 ALA A 101 PRO A 102 0 1.52
CISPEP 2 ALA B 101 PRO B 102 0 -1.81
SITE 1 AC1 13 HIS A 372 ASP A 375 GLN A 517 GLN A 518
SITE 2 AC1 13 ILE B 462 SER B 466 ASN B 485 ASN B 486
SITE 3 AC1 13 ASN B 504 GLU B 506 SER B 507 THR B 508
SITE 4 AC1 13 EDO B 604
SITE 1 AC2 13 ILE A 69 ASP A 70 TRP A 82 GLY A 116
SITE 2 AC2 13 GLY A 117 THR A 120 GLU A 197 SER A 198
SITE 3 AC2 13 ALA A 328 PHE A 329 TYR A 332 PHE A 398
SITE 4 AC2 13 HIS A 438
SITE 1 AC3 1 ARG A 135
SITE 1 AC4 1 LYS A 513
SITE 1 AC5 6 PRO A 189 LYS A 190 SER A 215 PHE A 217
SITE 2 AC5 6 THR A 218 LYS A 313
SITE 1 AC6 3 HIS A 77 MET A 81 GLU A 443
SITE 1 AC7 5 LEU A 18 TYR A 61 TRP A 98 ASP A 129
SITE 2 AC7 5 LYS A 131
SITE 1 AC8 6 SER A 466 ARG A 470 THR A 488 LEU A 503
SITE 2 AC8 6 THR A 508 CWQ B 601
SITE 1 AC9 4 GLN A 316 GLY A 413 ASN A 414 ASN A 415
SITE 1 AD1 3 ALA A 62 ASN A 63 TYR A 94
SITE 1 AD2 6 PRO A 230 TRP A 231 VAL A 233 GLU A 238
SITE 2 AD2 6 ARG A 242 VAL A 288
SITE 1 AD3 14 ILE A 462 SER A 466 ASN A 485 ASN A 486
SITE 2 AD3 14 ASN A 504 SER A 507 THR A 508 EDO A 608
SITE 3 AD3 14 HIS B 372 TYR B 373 ASP B 375 VAL B 377
SITE 4 AD3 14 GLN B 517 GLN B 518
SITE 1 AD4 9 ASN B 68 ASP B 70 TRP B 82 GLY B 116
SITE 2 AD4 9 GLY B 117 THR B 120 GLU B 197 SER B 198
SITE 3 AD4 9 HIS B 438
SITE 1 AD5 1 ARG B 515
SITE 1 AD6 5 CWQ A 601 SER B 466 ARG B 470 SER B 487
SITE 2 AD6 5 THR B 508
SITE 1 AD7 2 ARG B 14 ASN B 57
SITE 1 AD8 5 PRO B 230 THR B 234 GLU B 238 ARG B 242
SITE 2 AD8 5 VAL B 288
SITE 1 AD9 4 GLN B 316 GLY B 413 ASN B 414 ASN B 415
SITE 1 AE1 4 ARG A 14 ASP A 54 ILE A 55 ASN A 57
SITE 1 AE2 4 ASN A 106 ASN A 188 LYS A 190 HOH A 709
SITE 1 AE3 6 ASN A 241 ASN A 245 LEU A 249 PHE A 278
SITE 2 AE3 6 VAL A 279 PRO A 281
SITE 1 AE4 2 ASN A 341 ASN A 342
SITE 1 AE5 2 ARG A 465 ASN A 485
SITE 1 AE6 3 ASN B 106 ASN B 188 LYS B 190
SITE 1 AE7 7 ASN B 241 ASN B 245 LYS B 248 LEU B 249
SITE 2 AE7 7 PHE B 278 VAL B 279 PRO B 281
SITE 1 AE8 2 SER B 338 ASN B 341
SITE 1 AE9 4 ARG B 465 GLU B 482 ASN B 485 HOH B 732
CRYST1 152.140 152.140 141.910 90.00 90.00 90.00 P 4 21 2 16
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 0.006573 0.000000 0.000000 0.00000
SCALE2 0.000000 0.006573 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007047 0.00000
TER 4172 VAL A 529
TER 8362 VAL B 529
MASTER 452 0 37 50 29 0 46 6 8908 2 481 82
END |