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HEADER HYDROLASE 07-JAN-15 4XII
TITLE X-RAY STRUCTURE OF HUMAN BUTYRYLCHOLINESTERAS WIN COMPLEX WITH 3-
TITLE 2 PYRIDIN-4-YL-2,4-DIHYDRO-INDENO[1,2-.C.]PYRAZOLE
CAVEAT 4XII NAG A 1002 HAS WRONG CHIRALITY AT ATOM C1 FUL A 1005 HAS
CAVEAT 2 4XII WRONG CHIRALITY AT ATOM C1 NAG A 1011 HAS WRONG CHIRALITY
CAVEAT 3 4XII AT ATOM C1 NAG A 1015 HAS WRONG CHIRALITY AT ATOM C1 NAG B
CAVEAT 4 4XII 1008 HAS WRONG CHIRALITY AT ATOM 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: INSECT CELL EXPRESSION VECTOR PTIE1;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 266783
KEYWDS ANTI-ALZHERIMER, HUBUCHE, HUMAN BUTYRYLCHOLINESTERASE, METAL
KEYWDS 2 CHELATOR, ABETA PEPTIDE, AB AGGREGATION, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR D.KNEZ,B.BORIS,N.COQUELLE,I.SOSIC,R.SINK,X.BRAZZOLOTTO,J.MRAVLJAK,
AUTHOR 2 J.P.COLLETIER,S.GOBEC
REVDAT 1 08-JUL-15 4XII 0
JRNL AUTH D.KNEZ,B.BRUS,N.COQUELLE,I.SOSIC,R.SINK,X.BRAZZOLOTTO,
JRNL AUTH 2 J.MRAVLJAK,J.P.COLLETIER,S.GOBEC
JRNL TITL STRUCTURE-BASED DEVELOPMENT OF NITROXOLINE DERIVATIVES AS
JRNL TITL 2 POTENTIAL MULTIFUNCTIONAL ANTI-ALZHEIMER AGENTS.
JRNL REF BIOORG.MED.CHEM. 2015
JRNL REFN ESSN 1464-3391
JRNL PMID 26116179
JRNL DOI 10.1016/J.BMC.2015.06.010
REMARK 2
REMARK 2 RESOLUTION. 2.70 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.9_1692
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.70
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 46.19
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.350
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.0
REMARK 3 NUMBER OF REFLECTIONS : 39568
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.208
REMARK 3 R VALUE (WORKING SET) : 0.207
REMARK 3 FREE R VALUE : 0.257
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 3.810
REMARK 3 FREE R VALUE TEST SET COUNT : 1509
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 46.1974 - 6.0009 1.00 3715 148 0.1912 0.2078
REMARK 3 2 6.0009 - 4.7647 1.00 3549 139 0.1765 0.2111
REMARK 3 3 4.7647 - 4.1628 1.00 3522 140 0.1584 0.2118
REMARK 3 4 4.1628 - 3.7824 1.00 3477 133 0.1826 0.2761
REMARK 3 5 3.7824 - 3.5114 0.98 3395 129 0.2434 0.3252
REMARK 3 6 3.5114 - 3.3044 1.00 3462 143 0.2430 0.3078
REMARK 3 7 3.3044 - 3.1390 1.00 3477 139 0.2314 0.3310
REMARK 3 8 3.1390 - 3.0024 1.00 3414 134 0.2499 0.2693
REMARK 3 9 3.0024 - 2.8868 1.00 3463 131 0.2890 0.3454
REMARK 3 10 2.8868 - 2.7872 0.99 3415 135 0.3275 0.4026
REMARK 3 11 2.7872 - 2.7001 0.93 3170 138 0.3761 0.4087
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) : 0.450
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 30.360
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 9071
REMARK 3 ANGLE : 1.137 12283
REMARK 3 CHIRALITY : 0.044 1351
REMARK 3 PLANARITY : 0.005 1544
REMARK 3 DIHEDRAL : 14.615 3215
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 4XII COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 08-JAN-15.
REMARK 100 THE DEPOSITION ID IS D_1000205732.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 06-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 : ID23-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.006
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M-F
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 39583
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.701
REMARK 200 RESOLUTION RANGE LOW (A) : 46.800
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.0
REMARK 200 DATA REDUNDANCY : 3.000
REMARK 200 R MERGE (I) : 0.11100
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 11.9900
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.70
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.77
REMARK 200 COMPLETENESS FOR SHELL (%) : 91.9
REMARK 200 DATA REDUNDANCY IN SHELL : 4.20
REMARK 200 R MERGE FOR SHELL (I) : 1.83700
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: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 57.35
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.88
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 4000 12% 0.1M AMMONIUM ACETATE,
REMARK 280 VAPOR DIFFUSION, HANGING DROP, 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 38.52000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 115.43000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 39.88000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 115.43000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 38.52000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 39.88000
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: 9940 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 41120 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 57.0 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 A 531
REMARK 465 MET A 532
REMARK 465 THR A 533
REMARK 465 GLY A 534
REMARK 465 ASN A 535
REMARK 465 ILE A 536
REMARK 465 ASP A 537
REMARK 465 GLU A 538
REMARK 465 ALA A 539
REMARK 465 GLU A 540
REMARK 465 TRP A 541
REMARK 465 GLU A 542
REMARK 465 TRP A 543
REMARK 465 LYS A 544
REMARK 465 GLU B 1
REMARK 465 ASP B 2
REMARK 465 ASP B 3
REMARK 465 GLN B 484
REMARK 465 ASN B 485
REMARK 465 GLU B 531
REMARK 465 MET B 532
REMARK 465 THR B 533
REMARK 465 GLY B 534
REMARK 465 ASN B 535
REMARK 465 ILE B 536
REMARK 465 ASP B 537
REMARK 465 GLU B 538
REMARK 465 ALA B 539
REMARK 465 GLU B 540
REMARK 465 TRP B 541
REMARK 465 GLU B 542
REMARK 465 TRP B 543
REMARK 465 LYS B 544
REMARK 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 TYR A 237 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 GLU A 255 CG CD OE1 OE2
REMARK 470 TYR A 282 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 GLU A 506 CG CD OE1 OE2
REMARK 470 LEU A 530 CA C O CB CG CD1 CD2
REMARK 470 LYS B 51 CG CD CE NZ
REMARK 470 SER B 53 OG
REMARK 470 TYR B 282 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 ASN B 486 CG OD1 ND2
REMARK 470 SER B 507 CB OG
REMARK 470 LEU B 530 CA C O CB CG CD1 CD2
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 ND2 ASN A 481 O5 NAG A 1013 1.52
REMARK 500 ND2 ASN B 455 O5 NAG B 1009 1.53
REMARK 500 C6 NAG A 1003 C1 FUL A 1005 1.53
REMARK 500 O6 NAG B 1005 C1 FUL B 1006 1.61
REMARK 500 ND2 ASN A 241 O5 NAG A 1008 1.62
REMARK 500 OD1 ASN B 106 C1 NAG B 1004 1.64
REMARK 500 O6 NAG A 1008 C1 FUL A 1010 1.69
REMARK 500 ND2 ASN B 17 C2 NAG B 1002 1.78
REMARK 500 ND2 ASN A 57 C1 NAG A 1003 1.82
REMARK 500 O6 NAG A 1003 C2 FUL A 1005 1.84
REMARK 500 ND2 ASN B 241 C1 NAG B 1005 1.88
REMARK 500 O6 NAG A 1015 C1 FUL A 1017 1.88
REMARK 500 O4 NAG A 1006 O5 NAG A 1007 1.88
REMARK 500 ND2 ASN A 341 O5 NAG A 1011 1.89
REMARK 500 O GLY A 116 O HOH A 1101 1.94
REMARK 500 ND2 ASN A 17 O5 NAG A 1002 1.95
REMARK 500 ND2 ASN A 486 O5 NAG A 1015 1.96
REMARK 500 ND2 ASN B 57 C2 NAG B 1003 2.02
REMARK 500 O6 NAG A 1011 O5 FUC A 1012 2.02
REMARK 500 O6 NAG A 1003 O2 FUL A 1005 2.09
REMARK 500 OG SER A 123 OD1 ASN A 145 2.10
REMARK 500 CG ASN A 241 C1 NAG A 1008 2.11
REMARK 500 NH2 ARG B 240 OE2 GLU B 257 2.13
REMARK 500 ND2 ASN A 106 O5 NAG A 1006 2.15
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 PRO B 382 C - N - CA ANGL. DEV. = 21.4 DEGREES
REMARK 500 PRO B 382 C - N - CD ANGL. DEV. = -18.4 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 THR A 50 -91.08 -90.61
REMARK 500 ASP A 54 -150.23 -84.14
REMARK 500 ASN A 106 49.08 -149.81
REMARK 500 ALA A 162 78.54 -167.26
REMARK 500 SER A 198 -117.48 60.72
REMARK 500 TYR A 282 -84.60 -75.05
REMARK 500 ASP A 297 -74.83 -123.62
REMARK 500 ARG A 381 78.26 54.96
REMARK 500 PHE A 398 -56.38 -128.05
REMARK 500 TYR A 440 30.67 -99.22
REMARK 500 PRO A 480 44.08 -78.63
REMARK 500 GLU A 482 -70.71 -99.44
REMARK 500 GLU A 506 -78.94 -68.49
REMARK 500 ARG A 515 42.90 36.73
REMARK 500 PHE A 525 -46.85 -132.98
REMARK 500 ASP B 54 -151.32 -83.20
REMARK 500 SER B 89 146.98 -170.97
REMARK 500 PRO B 102 -174.95 -63.12
REMARK 500 ASN B 106 58.88 -153.44
REMARK 500 PRO B 160 -2.43 -59.25
REMARK 500 ALA B 162 78.98 -167.91
REMARK 500 SER B 198 -117.41 59.86
REMARK 500 TYR B 282 36.10 -78.68
REMARK 500 ASP B 297 -73.49 -122.20
REMARK 500 GLN B 380 -71.20 -76.44
REMARK 500 ARG B 381 -90.36 55.61
REMARK 500 GLU B 383 2.71 -69.65
REMARK 500 PHE B 398 -57.01 -128.42
REMARK 500 PRO B 480 42.26 -80.42
REMARK 500 GLU B 482 -147.82 -102.20
REMARK 500 GLU B 506 -81.03 -68.15
REMARK 500 ARG B 515 42.99 36.15
REMARK 500 PHE B 525 -47.01 -133.18
REMARK 500
REMARK 500 REMARK: NULL
REMARK 610
REMARK 610 MISSING HETEROATOM
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 610 I=INSERTION CODE):
REMARK 610 M RES C SSEQI
REMARK 610 NAG A 1003
REMARK 610 FUL A 1010
REMARK 610 FUC A 1012
REMARK 610 FUL A 1017
REMARK 610 NAG B 1004
REMARK 610 NAG B 1005
REMARK 610 FUL B 1006
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 40V A 1001
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue FUL A 1010
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue FUC A 1012
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue FUL A 1017
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 1019
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 1020
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 1021
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 1022
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 40V B 1001
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue NAG B 1004
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue NAG B 1005
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue FUL B 1006
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL B 1011
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 1012
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 1013
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG A 1002
REMARK 800 bound to ASN A 17
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG A
REMARK 800 1006 through NAG A 1007 bound to ASN A 106
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG A
REMARK 800 1008 through NAG A 1009 bound to ASN A 241
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG A 1011
REMARK 800 bound to ASN A 341
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG A
REMARK 800 1013 through NAG A 1014 bound to ASN A 481
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 1015 through NAG A 1016 bound to ASN A 486
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG B 1002
REMARK 800 bound to ASN B 17
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG B 1003
REMARK 800 bound to ASN B 57
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG B 1007
REMARK 800 bound to ASN B 256
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG B 1008
REMARK 800 bound to ASN B 341
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG B 1009
REMARK 800 bound to ASN B 455
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG B 1010
REMARK 800 bound to ASN B 481
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 1003 through FUL A 1005
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4TPK RELATED DB: PDB
REMARK 900 4TPK CONTAINS THE SAME PROTEIN COMPLEXED WITH A SIMILAR INHIBITOR.
DBREF 4XII A 1 544 UNP P06276 CHLE_HUMAN 29 572
DBREF 4XII B 1 544 UNP P06276 CHLE_HUMAN 29 572
SEQRES 1 A 544 GLU ASP ASP ILE ILE ILE ALA THR LYS ASN GLY LYS VAL
SEQRES 2 A 544 ARG GLY MET ASN LEU THR VAL PHE GLY GLY THR VAL THR
SEQRES 3 A 544 ALA PHE LEU GLY ILE PRO TYR ALA GLN PRO PRO LEU GLY
SEQRES 4 A 544 ARG LEU ARG PHE LYS LYS PRO GLN SER LEU THR LYS TRP
SEQRES 5 A 544 SER ASP ILE TRP ASN ALA THR LYS TYR ALA ASN SER CYS
SEQRES 6 A 544 CYS GLN ASN ILE ASP GLN SER PHE PRO GLY PHE HIS GLY
SEQRES 7 A 544 SER GLU MET TRP ASN PRO ASN THR ASP LEU SER GLU ASP
SEQRES 8 A 544 CYS LEU TYR LEU ASN VAL TRP ILE PRO ALA PRO LYS PRO
SEQRES 9 A 544 LYS ASN ALA THR VAL LEU ILE TRP ILE TYR GLY GLY GLY
SEQRES 10 A 544 PHE GLN THR GLY THR SER SER LEU HIS VAL TYR ASP GLY
SEQRES 11 A 544 LYS PHE LEU ALA ARG VAL GLU ARG VAL ILE VAL VAL SER
SEQRES 12 A 544 MET ASN TYR ARG VAL GLY ALA LEU GLY PHE LEU ALA LEU
SEQRES 13 A 544 PRO GLY ASN PRO GLU ALA PRO GLY ASN MET GLY LEU PHE
SEQRES 14 A 544 ASP GLN GLN LEU ALA LEU GLN TRP VAL GLN LYS ASN ILE
SEQRES 15 A 544 ALA ALA PHE GLY GLY ASN PRO LYS SER VAL THR LEU PHE
SEQRES 16 A 544 GLY GLU SER ALA GLY ALA ALA SER VAL SER LEU HIS LEU
SEQRES 17 A 544 LEU SER PRO GLY SER HIS SER LEU PHE THR ARG ALA ILE
SEQRES 18 A 544 LEU GLN SER GLY SER PHE ASN ALA PRO TRP ALA VAL THR
SEQRES 19 A 544 SER LEU TYR GLU ALA ARG ASN ARG THR LEU ASN LEU ALA
SEQRES 20 A 544 LYS LEU THR GLY CYS SER ARG GLU ASN GLU THR GLU ILE
SEQRES 21 A 544 ILE LYS CYS LEU ARG ASN LYS ASP PRO GLN GLU ILE LEU
SEQRES 22 A 544 LEU ASN GLU ALA PHE VAL VAL PRO TYR GLY THR PRO LEU
SEQRES 23 A 544 SER VAL ASN PHE GLY PRO THR VAL ASP GLY ASP PHE LEU
SEQRES 24 A 544 THR ASP MET PRO ASP ILE LEU LEU GLU LEU GLY GLN PHE
SEQRES 25 A 544 LYS LYS THR GLN ILE LEU VAL GLY VAL ASN LYS ASP GLU
SEQRES 26 A 544 GLY THR ALA PHE LEU VAL TYR GLY ALA PRO GLY PHE SER
SEQRES 27 A 544 LYS ASP ASN ASN SER ILE ILE THR ARG LYS GLU PHE GLN
SEQRES 28 A 544 GLU GLY LEU LYS ILE PHE PHE PRO GLY VAL SER GLU PHE
SEQRES 29 A 544 GLY LYS GLU SER ILE LEU PHE HIS TYR THR ASP TRP VAL
SEQRES 30 A 544 ASP ASP GLN ARG PRO GLU ASN TYR ARG GLU ALA LEU GLY
SEQRES 31 A 544 ASP VAL VAL GLY ASP TYR ASN PHE ILE CYS PRO ALA LEU
SEQRES 32 A 544 GLU PHE THR LYS LYS PHE SER GLU TRP GLY ASN ASN ALA
SEQRES 33 A 544 PHE PHE TYR TYR PHE GLU HIS ARG SER SER LYS LEU PRO
SEQRES 34 A 544 TRP PRO GLU TRP MET GLY VAL MET HIS GLY TYR GLU ILE
SEQRES 35 A 544 GLU PHE VAL PHE GLY LEU PRO LEU GLU ARG ARG ASP ASN
SEQRES 36 A 544 TYR THR LYS ALA GLU GLU ILE LEU SER ARG SER ILE VAL
SEQRES 37 A 544 LYS ARG TRP ALA ASN PHE ALA LYS TYR GLY ASN PRO ASN
SEQRES 38 A 544 GLU THR GLN ASN ASN SER THR SER TRP PRO VAL PHE LYS
SEQRES 39 A 544 SER THR GLU GLN LYS TYR LEU THR LEU ASN THR GLU SER
SEQRES 40 A 544 THR ARG ILE MET THR LYS LEU ARG ALA GLN GLN CYS ARG
SEQRES 41 A 544 PHE TRP THR SER PHE PHE PRO LYS VAL LEU GLU MET THR
SEQRES 42 A 544 GLY ASN ILE ASP GLU ALA GLU TRP GLU TRP LYS
SEQRES 1 B 544 GLU ASP ASP ILE ILE ILE ALA THR LYS ASN GLY LYS VAL
SEQRES 2 B 544 ARG GLY MET ASN LEU THR VAL PHE GLY GLY THR VAL THR
SEQRES 3 B 544 ALA PHE LEU GLY ILE PRO TYR ALA GLN PRO PRO LEU GLY
SEQRES 4 B 544 ARG LEU ARG PHE LYS LYS PRO GLN SER LEU THR LYS TRP
SEQRES 5 B 544 SER ASP ILE TRP ASN ALA THR LYS TYR ALA ASN SER CYS
SEQRES 6 B 544 CYS GLN ASN ILE ASP GLN SER PHE PRO GLY PHE HIS GLY
SEQRES 7 B 544 SER GLU MET TRP ASN PRO ASN THR ASP LEU SER GLU ASP
SEQRES 8 B 544 CYS LEU TYR LEU ASN VAL TRP ILE PRO ALA PRO LYS PRO
SEQRES 9 B 544 LYS ASN ALA THR VAL LEU ILE TRP ILE TYR GLY GLY GLY
SEQRES 10 B 544 PHE GLN THR GLY THR SER SER LEU HIS VAL TYR ASP GLY
SEQRES 11 B 544 LYS PHE LEU ALA ARG VAL GLU ARG VAL ILE VAL VAL SER
SEQRES 12 B 544 MET ASN TYR ARG VAL GLY ALA LEU GLY PHE LEU ALA LEU
SEQRES 13 B 544 PRO GLY ASN PRO GLU ALA PRO GLY ASN MET GLY LEU PHE
SEQRES 14 B 544 ASP GLN GLN LEU ALA LEU GLN TRP VAL GLN LYS ASN ILE
SEQRES 15 B 544 ALA ALA PHE GLY GLY ASN PRO LYS SER VAL THR LEU PHE
SEQRES 16 B 544 GLY GLU SER ALA GLY ALA ALA SER VAL SER LEU HIS LEU
SEQRES 17 B 544 LEU SER PRO GLY SER HIS SER LEU PHE THR ARG ALA ILE
SEQRES 18 B 544 LEU GLN SER GLY SER PHE ASN ALA PRO TRP ALA VAL THR
SEQRES 19 B 544 SER LEU TYR GLU ALA ARG ASN ARG THR LEU ASN LEU ALA
SEQRES 20 B 544 LYS LEU THR GLY CYS SER ARG GLU ASN GLU THR GLU ILE
SEQRES 21 B 544 ILE LYS CYS LEU ARG ASN LYS ASP PRO GLN GLU ILE LEU
SEQRES 22 B 544 LEU ASN GLU ALA PHE VAL VAL PRO TYR GLY THR PRO LEU
SEQRES 23 B 544 SER VAL ASN PHE GLY PRO THR VAL ASP GLY ASP PHE LEU
SEQRES 24 B 544 THR ASP MET PRO ASP ILE LEU LEU GLU LEU GLY GLN PHE
SEQRES 25 B 544 LYS LYS THR GLN ILE LEU VAL GLY VAL ASN LYS ASP GLU
SEQRES 26 B 544 GLY THR ALA PHE LEU VAL TYR GLY ALA PRO GLY PHE SER
SEQRES 27 B 544 LYS ASP ASN ASN SER ILE ILE THR ARG LYS GLU PHE GLN
SEQRES 28 B 544 GLU GLY LEU LYS ILE PHE PHE PRO GLY VAL SER GLU PHE
SEQRES 29 B 544 GLY LYS GLU SER ILE LEU PHE HIS TYR THR ASP TRP VAL
SEQRES 30 B 544 ASP ASP GLN ARG PRO GLU ASN TYR ARG GLU ALA LEU GLY
SEQRES 31 B 544 ASP VAL VAL GLY ASP TYR ASN PHE ILE CYS PRO ALA LEU
SEQRES 32 B 544 GLU PHE THR LYS LYS PHE SER GLU TRP GLY ASN ASN ALA
SEQRES 33 B 544 PHE PHE TYR TYR PHE GLU HIS ARG SER SER LYS LEU PRO
SEQRES 34 B 544 TRP PRO GLU TRP MET GLY VAL MET HIS GLY TYR GLU ILE
SEQRES 35 B 544 GLU PHE VAL PHE GLY LEU PRO LEU GLU ARG ARG ASP ASN
SEQRES 36 B 544 TYR THR LYS ALA GLU GLU ILE LEU SER ARG SER ILE VAL
SEQRES 37 B 544 LYS ARG TRP ALA ASN PHE ALA LYS TYR GLY ASN PRO ASN
SEQRES 38 B 544 GLU THR GLN ASN ASN SER THR SER TRP PRO VAL PHE LYS
SEQRES 39 B 544 SER THR GLU GLN LYS TYR LEU THR LEU ASN THR GLU SER
SEQRES 40 B 544 THR ARG ILE MET THR LYS LEU ARG ALA GLN GLN CYS ARG
SEQRES 41 B 544 PHE TRP THR SER PHE PHE PRO LYS VAL LEU GLU MET THR
SEQRES 42 B 544 GLY ASN ILE ASP GLU ALA GLU TRP GLU TRP LYS
HET 40V A1001 37
HET NAG A1002 14
HET NAG A1003 14
HET NAG A1004 14
HET FUL A1005 10
HET NAG A1006 14
HET NAG A1007 14
HET NAG A1008 14
HET NAG A1009 14
HET FUL A1010 10
HET NAG A1011 14
HET FUC A1012 10
HET NAG A1013 14
HET NAG A1014 14
HET NAG A1015 14
HET NAG A1016 14
HET FUL A1017 10
HET CL A1018 1
HET CL A1019 1
HET CL A1020 1
HET EDO A1021 4
HET EDO A1022 4
HET 40V B1001 37
HET NAG B1002 14
HET NAG B1003 14
HET NAG B1004 14
HET NAG B1005 14
HET FUL B1006 10
HET NAG B1007 14
HET NAG B1008 14
HET NAG B1009 14
HET NAG B1010 14
HET CL B1011 1
HET EDO B1012 4
HET EDO B1013 4
HETNAM 40V N-{[(3R)-1-(2,3-DIHYDRO-1H-INDEN-2-YL)PIPERIDIN-3-
HETNAM 2 40V YL]METHYL}-8-HYDROXY-N-(2-METHOXYETHYL)-5-
HETNAM 3 40V NITROQUINOLINE-7-CARBOXAMIDE
HETNAM NAG N-ACETYL-D-GLUCOSAMINE
HETNAM FUL BETA-L-FUCOSE
HETNAM FUC ALPHA-L-FUCOSE
HETNAM CL CHLORIDE ION
HETNAM EDO 1,2-ETHANEDIOL
HETSYN FUL 6-DEOXY-BETA-L-GALACTOSE
HETSYN EDO ETHYLENE GLYCOL
FORMUL 3 40V 2(C28 H32 N4 O5)
FORMUL 4 NAG 20(C8 H15 N O6)
FORMUL 5 FUL 4(C6 H12 O5)
FORMUL 10 FUC C6 H12 O5
FORMUL 14 CL 4(CL 1-)
FORMUL 17 EDO 4(C2 H6 O2)
FORMUL 32 HOH *62(H2 O)
HELIX 1 AA1 LEU A 38 ARG A 42 5 5
HELIX 2 AA2 PHE A 76 MET A 81 1 6
HELIX 3 AA3 LEU A 125 ASP A 129 5 5
HELIX 4 AA4 GLY A 130 ARG A 138 1 9
HELIX 5 AA5 GLY A 149 LEU A 154 1 6
HELIX 6 AA6 ASN A 165 ILE A 182 1 18
HELIX 7 AA7 ALA A 183 PHE A 185 5 3
HELIX 8 AA8 SER A 198 SER A 210 1 13
HELIX 9 AA9 PRO A 211 PHE A 217 5 7
HELIX 10 AB1 SER A 235 GLY A 251 1 17
HELIX 11 AB2 ASN A 256 ARG A 265 1 10
HELIX 12 AB3 ASP A 268 LEU A 274 1 7
HELIX 13 AB4 ASN A 275 VAL A 280 5 6
HELIX 14 AB5 MET A 302 LEU A 309 1 8
HELIX 15 AB6 GLY A 326 VAL A 331 1 6
HELIX 16 AB7 THR A 346 PHE A 358 1 13
HELIX 17 AB8 PHE A 364 TYR A 373 1 10
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 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 GLY B 310 1 9
HELIX 40 AE4 GLY B 326 VAL B 331 1 6
HELIX 41 AE5 THR B 346 PHE B 358 1 13
HELIX 42 AE6 PHE B 364 TYR B 373 1 10
HELIX 43 AE7 GLU B 383 PHE B 398 1 16
HELIX 44 AE8 PHE B 398 GLU B 411 1 14
HELIX 45 AE9 PRO B 431 GLY B 435 5 5
HELIX 46 AF1 GLU B 441 PHE B 446 1 6
HELIX 47 AF2 GLY B 447 ASN B 455 5 9
HELIX 48 AF3 THR B 457 GLY B 478 1 22
HELIX 49 AF4 ARG B 515 PHE B 525 1 11
HELIX 50 AF5 PHE B 526 VAL B 529 5 4
SHEET 1 AA1 3 ILE A 5 THR A 8 0
SHEET 2 AA1 3 GLY A 11 ARG A 14 -1 O GLY A 11 N THR A 8
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 VAL A 97 N PHE A 28
SHEET 4 AA211 ILE A 140 MET A 144 -1 O SER A 143 N ASN A 96
SHEET 5 AA211 ALA A 107 ILE A 113 1 N LEU A 110 O ILE A 140
SHEET 6 AA211 GLY A 187 GLU A 197 1 O THR A 193 N ILE A 111
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 503 N TYR A 420
SHEET 11 AA211 ILE A 510 THR A 512 -1 O MET A 511 N TYR A 500
SHEET 1 AA3 3 ILE B 5 THR B 8 0
SHEET 2 AA3 3 GLY B 11 ARG B 14 -1 O VAL B 13 N ILE B 6
SHEET 3 AA3 3 ILE B 55 ASN B 57 1 O TRP B 56 N LYS B 12
SHEET 1 AA411 MET B 16 VAL B 20 0
SHEET 2 AA411 GLY B 23 PRO B 32 -1 O ALA B 27 N MET B 16
SHEET 3 AA411 TYR B 94 ALA B 101 -1 O VAL B 97 N PHE B 28
SHEET 4 AA411 ILE B 140 MET B 144 -1 O SER B 143 N ASN B 96
SHEET 5 AA411 ALA B 107 ILE B 113 1 N TRP B 112 O VAL B 142
SHEET 6 AA411 GLY B 187 GLU B 197 1 O ASN B 188 N ALA B 107
SHEET 7 AA411 ARG B 219 GLN B 223 1 O ARG B 219 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 501 N PHE B 418
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 2.02
SSBOND 2 CYS A 252 CYS A 263 1555 1555 2.04
SSBOND 3 CYS A 400 CYS A 519 1555 1555 2.05
SSBOND 4 CYS B 65 CYS B 92 1555 1555 2.04
SSBOND 5 CYS B 252 CYS B 263 1555 1555 2.04
SSBOND 6 CYS B 400 CYS B 519 1555 1555 2.05
LINK ND2 ASN A 17 C1 NAG A1002 1555 1555 1.47
LINK ND2 ASN A 106 C1 NAG A1006 1555 1555 1.43
LINK ND2 ASN A 241 C1 NAG A1008 1555 1555 1.48
LINK ND2 ASN A 341 C1 NAG A1011 1555 1555 1.48
LINK ND2 ASN A 481 C1 NAG A1013 1555 1555 1.47
LINK ND2 ASN A 486 C1 NAG A1015 1555 1555 1.47
LINK ND2 ASN B 17 C1 NAG B1002 1555 1555 1.34
LINK ND2 ASN B 57 C1 NAG B1003 1555 1555 1.40
LINK ND2 ASN B 256 C1 NAG B1007 1555 1555 1.38
LINK ND2 ASN B 341 C1 NAG B1008 1555 1555 1.41
LINK ND2 ASN B 455 C1 NAG B1009 1555 1555 1.54
LINK ND2 ASN B 481 O5 NAG B1010 1555 1555 1.49
LINK ND2 ASN B 481 C1 NAG B1010 1555 1555 1.48
LINK O4 NAG A1003 C1 NAG A1004 1555 1555 1.45
LINK O6 NAG A1003 C1 FUL A1005 1555 1555 1.13
LINK O4 NAG A1006 C1 NAG A1007 1555 1555 1.50
LINK O4 NAG A1008 C1 NAG A1009 1555 1555 1.49
LINK O4 NAG A1013 C1 NAG A1014 1555 1555 1.46
LINK O4 NAG A1015 C1 NAG A1016 1555 1555 1.48
CISPEP 1 ALA A 101 PRO A 102 0 4.02
CISPEP 2 GLN A 380 ARG A 381 0 -12.78
CISPEP 3 ALA B 101 PRO B 102 0 0.03
CISPEP 4 ARG B 381 PRO B 382 0 -3.52
SITE 1 AC1 17 ASN A 68 ILE A 69 ASP A 70 TRP A 82
SITE 2 AC1 17 GLY A 116 GLY A 117 GLU A 197 SER A 198
SITE 3 AC1 17 TRP A 231 PRO A 285 SER A 287 PHE A 329
SITE 4 AC1 17 TYR A 332 PHE A 398 HIS A 438 HOH A1101
SITE 5 AC1 17 HOH A1123
SITE 1 AC2 5 ASN A 245 PHE A 278 PRO A 281 NAG A1008
SITE 2 AC2 5 NAG A1009
SITE 1 AC3 1 NAG A1011
SITE 1 AC4 5 GLU A 482 SER A 487 THR A 488 NAG A1015
SITE 2 AC4 5 NAG A1016
SITE 1 AC5 5 ARG A 470 ASN A 481 THR A 488 TRP A 490
SITE 2 AC5 5 HOH A1117
SITE 1 AC6 2 ARG A 386 HOH A1135
SITE 1 AC7 3 ARG A 386 GLU A 387 TRP A 433
SITE 1 AC8 5 PRO A 104 LYS A 105 ASN A 106 ALA A 107
SITE 2 AC8 5 ARG A 138
SITE 1 AC9 17 ILE B 69 ASP B 70 TRP B 82 GLY B 116
SITE 2 AC9 17 GLY B 117 GLU B 197 SER B 198 TRP B 231
SITE 3 AC9 17 PRO B 285 LEU B 286 SER B 287 PHE B 329
SITE 4 AC9 17 TYR B 332 HIS B 438 EDO B1013 HOH B1101
SITE 5 AC9 17 HOH B1120
SITE 1 AD1 5 ASN B 106 ASN B 188 LYS B 190 HOH B1107
SITE 2 AD1 5 HOH B1117
SITE 1 AD2 5 TYR B 237 ASN B 241 ASN B 245 FUL B1006
SITE 2 AD2 5 HOH B1106
SITE 1 AD3 4 ASN B 245 LEU B 249 PHE B 278 NAG B1005
SITE 1 AD4 1 ARG B 242
SITE 1 AD5 6 GLN A 316 ASN A 414 ASN B 266 LYS B 267
SITE 2 AD5 6 ASP B 268 GLU B 271
SITE 1 AD6 3 ASN B 68 40V B1001 HOH B1112
SITE 1 AD7 1 ASN A 17
SITE 1 AD8 2 ASN A 106 ASN A 188
SITE 1 AD9 3 ASN A 241 ASN A 245 FUL A1010
SITE 1 AE1 5 GLY A 336 SER A 338 ASN A 341 ILE A 344
SITE 2 AE1 5 FUC A1012
SITE 1 AE2 8 TYR A 477 ASN A 479 ASN A 481 GLU A 482
SITE 2 AE2 8 THR A 483 GLN A 484 LEU B 88 GLN B 270
SITE 1 AE3 2 ASN A 486 FUL A1017
SITE 1 AE4 2 ILE B 4 ASN B 17
SITE 1 AE5 2 ARG B 14 ASN B 57
SITE 1 AE6 4 ASN B 256 GLU B 259 GLU B 411 HOH B1102
SITE 1 AE7 8 GLY B 336 SER B 338 ASN B 341 ASN B 342
SITE 2 AE7 8 SER B 343 ILE B 344 HOH B1111 HOH B1123
SITE 1 AE8 2 ASP B 454 ASN B 455
SITE 1 AE9 2 ASN B 481 GLU B 482
SITE 1 AF1 2 ARG A 14 ASN A 57
CRYST1 77.040 79.760 230.860 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 0.012980 0.000000 0.000000 0.00000
SCALE2 0.000000 0.012538 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004332 0.00000
TER 4196 LEU A 530
TER 8365 LEU B 530
MASTER 507 0 35 50 28 0 46 6 8820 2 444 84
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