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HEADER HYDROLASE 07-APR-17 5NN0
TITLE CRYSTAL STRUCTURE OF HUBCHE WITH N-((1-(2,3-DIHYDRO-1H-INDEN-2-YL)
TITLE 2 PIPERIDIN-3-YL)METHYL)-N-(2-(DIMETHYLAMINO)ETHYL)-2-NAPHTHAMIDE.
CAVEAT 5NN0 FUC A 605 HAS WRONG CHIRALITY AT ATOM C1 NAG A 608 HAS WRONG
CAVEAT 2 5NN0 CHIRALITY AT ATOM C1
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CHOLINESTERASE;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: ACYLCHOLINE ACYLHYDROLASE,BUTYRYLCHOLINE ESTERASE,CHOLINE
COMPND 5 ESTERASE II,PSEUDOCHOLINESTERASE;
COMPND 6 EC: 3.1.1.8;
COMPND 7 ENGINEERED: YES;
COMPND 8 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: BCHE, CHE1;
SOURCE 6 EXPRESSION_SYSTEM: CRICETULUS GRISEUS;
SOURCE 7 EXPRESSION_SYSTEM_COMMON: CHINESE HAMSTER;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 10029
KEYWDS BUTYRYLCHOLINESTERASE AD ALZHEIMER DISEASE INHIBITOR, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR N.COQUELLE,B.BRUS,J.P.COLLETIER
REVDAT 1 14-MAR-18 5NN0 0
JRNL AUTH U.KOSAK,B.BRUS,D.KNEZ,S.ZAKELJ,J.TRONTELJ,A.PISLAR,R.SINK,
JRNL AUTH 2 M.JUKIC,M.ZIVIN,A.PODKOWA,F.NACHON,X.BRAZZOLOTTO,J.STOJAN,
JRNL AUTH 3 J.KOS,N.COQUELLE,K.SALAT,J.P.COLLETIER,S.GOBEC
JRNL TITL THE MAGIC OF CRYSTAL STRUCTURE-BASED INHIBITOR OPTIMIZATION:
JRNL TITL 2 DEVELOPMENT OF A BUTYRYLCHOLINESTERASE INHIBITOR WITH
JRNL TITL 3 PICOMOLAR AFFINITY AND IN VIVO ACTIVITY.
JRNL REF J. MED. CHEM. V. 61 119 2018
JRNL REFN ISSN 1520-4804
JRNL PMID 29227101
JRNL DOI 10.1021/ACS.JMEDCHEM.7B01086
REMARK 2
REMARK 2 RESOLUTION. 2.10 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) : 2.10
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 47.83
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.350
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.2
REMARK 3 NUMBER OF REFLECTIONS : 44731
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.171
REMARK 3 R VALUE (WORKING SET) : 0.169
REMARK 3 FREE R VALUE : 0.206
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 2237
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 47.8451 - 5.2894 0.97 2775 147 0.1871 0.2187
REMARK 3 2 5.2894 - 4.1991 0.98 2688 141 0.1363 0.1614
REMARK 3 3 4.1991 - 3.6686 0.99 2674 141 0.1360 0.1601
REMARK 3 4 3.6686 - 3.3332 0.99 2634 138 0.1481 0.1825
REMARK 3 5 3.3332 - 3.0944 0.99 2684 142 0.1556 0.2108
REMARK 3 6 3.0944 - 2.9120 0.99 2628 138 0.1716 0.2044
REMARK 3 7 2.9120 - 2.7661 0.99 2650 140 0.1679 0.1964
REMARK 3 8 2.7661 - 2.6457 1.00 2652 139 0.1824 0.2297
REMARK 3 9 2.6457 - 2.5439 1.00 2640 139 0.1875 0.2752
REMARK 3 10 2.5439 - 2.4561 1.00 2639 139 0.1908 0.2436
REMARK 3 11 2.4561 - 2.3793 1.00 2638 139 0.1957 0.2200
REMARK 3 12 2.3793 - 2.3113 1.00 2640 139 0.2034 0.2534
REMARK 3 13 2.3113 - 2.2505 1.00 2630 138 0.2106 0.2597
REMARK 3 14 2.2505 - 2.1956 1.00 2650 140 0.2259 0.3045
REMARK 3 15 2.1956 - 2.1456 1.00 2604 137 0.2372 0.2515
REMARK 3 16 2.1456 - 2.1000 1.00 2668 140 0.2433 0.2955
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) : 0.220
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 20.610
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 4685
REMARK 3 ANGLE : 0.877 6373
REMARK 3 CHIRALITY : 0.051 690
REMARK 3 PLANARITY : 0.005 789
REMARK 3 DIHEDRAL : 10.710 3684
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 5NN0 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 07-APR-17.
REMARK 100 THE DEPOSITION ID IS D_1200004354.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 04-NOV-15
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.5
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 : 183875
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.100
REMARK 200 RESOLUTION RANGE LOW (A) : 47.833
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.4
REMARK 200 DATA REDUNDANCY : 4.120
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 10.9800
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.10
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.18
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.7
REMARK 200 DATA REDUNDANCY IN SHELL : 3.90
REMARK 200 R MERGE FOR SHELL (I) : 1.00200
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 1.500
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 (%): 61.33
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.18
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M MES PH 6.5 2.3 M AMMONIUM
REMARK 280 SULFATE, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 4 2 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,X,Z
REMARK 290 4555 Y,-X,Z
REMARK 290 5555 -X,Y,-Z
REMARK 290 6555 X,-Y,-Z
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -Y,-X,-Z
REMARK 290 9555 X+1/2,Y+1/2,Z+1/2
REMARK 290 10555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 11555 -Y+1/2,X+1/2,Z+1/2
REMARK 290 12555 Y+1/2,-X+1/2,Z+1/2
REMARK 290 13555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 14555 X+1/2,-Y+1/2,-Z+1/2
REMARK 290 15555 Y+1/2,X+1/2,-Z+1/2
REMARK 290 16555 -Y+1/2,-X+1/2,-Z+1/2
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 0.00000
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 0.00000
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 SMTRY1 9 1.000000 0.000000 0.000000 77.48500
REMARK 290 SMTRY2 9 0.000000 1.000000 0.000000 77.48500
REMARK 290 SMTRY3 9 0.000000 0.000000 1.000000 63.34000
REMARK 290 SMTRY1 10 -1.000000 0.000000 0.000000 77.48500
REMARK 290 SMTRY2 10 0.000000 -1.000000 0.000000 77.48500
REMARK 290 SMTRY3 10 0.000000 0.000000 1.000000 63.34000
REMARK 290 SMTRY1 11 0.000000 -1.000000 0.000000 77.48500
REMARK 290 SMTRY2 11 1.000000 0.000000 0.000000 77.48500
REMARK 290 SMTRY3 11 0.000000 0.000000 1.000000 63.34000
REMARK 290 SMTRY1 12 0.000000 1.000000 0.000000 77.48500
REMARK 290 SMTRY2 12 -1.000000 0.000000 0.000000 77.48500
REMARK 290 SMTRY3 12 0.000000 0.000000 1.000000 63.34000
REMARK 290 SMTRY1 13 -1.000000 0.000000 0.000000 77.48500
REMARK 290 SMTRY2 13 0.000000 1.000000 0.000000 77.48500
REMARK 290 SMTRY3 13 0.000000 0.000000 -1.000000 63.34000
REMARK 290 SMTRY1 14 1.000000 0.000000 0.000000 77.48500
REMARK 290 SMTRY2 14 0.000000 -1.000000 0.000000 77.48500
REMARK 290 SMTRY3 14 0.000000 0.000000 -1.000000 63.34000
REMARK 290 SMTRY1 15 0.000000 1.000000 0.000000 77.48500
REMARK 290 SMTRY2 15 1.000000 0.000000 0.000000 77.48500
REMARK 290 SMTRY3 15 0.000000 0.000000 -1.000000 63.34000
REMARK 290 SMTRY1 16 0.000000 -1.000000 0.000000 77.48500
REMARK 290 SMTRY2 16 -1.000000 0.000000 0.000000 77.48500
REMARK 290 SMTRY3 16 0.000000 0.000000 -1.000000 63.34000
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: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 6510 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 20950 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -36.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH A 966 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A1009 LIES ON A SPECIAL POSITION.
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 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 LYS A 51 CG CD CE NZ
REMARK 470 LYS A 60 CD CE NZ
REMARK 470 LYS A 262 CD CE NZ
REMARK 470 TYR A 282 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 ASP A 379 CG OD1 OD2
REMARK 470 GLN A 380 CG CD OE1 NE2
REMARK 470 GLU A 432 CD OE1 OE2
REMARK 470 ARG A 452 CG CD NE CZ NH1 NH2
REMARK 470 ARG A 453 CG CD 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 C6 NAG A 609 C1 FUC A 611 1.93
REMARK 500 O6 NAG A 609 C2 FUC A 611 2.08
REMARK 500 O HOH A 851 O HOH A 915 2.15
REMARK 500 OG1 THR A 508 O HOH A 702 2.18
REMARK 500 OE1 GLU A 238 O HOH A 703 2.19
REMARK 500 NE2 HIS A 372 O4 SO4 A 620 2.19
REMARK 500 O6 NAG A 604 O5 FUC A 605 2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 PHE A 43 -1.70 73.59
REMARK 500 ALA A 58 63.50 -101.26
REMARK 500 ASN A 106 58.93 -152.53
REMARK 500 ALA A 162 71.09 -151.94
REMARK 500 SER A 198 -119.22 51.50
REMARK 500 SER A 198 -120.26 53.14
REMARK 500 ASP A 297 -74.43 -132.10
REMARK 500 VAL A 377 -84.76 -47.22
REMARK 500 PHE A 398 -53.39 -133.22
REMARK 500 ARG A 453 3.59 -66.77
REMARK 500 ASN A 485 51.13 -105.46
REMARK 500 ASN A 486 44.02 37.69
REMARK 500 GLU A 506 -88.31 -64.11
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 A1014 DISTANCE = 6.05 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 612
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 613
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 614
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 615
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 616
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 619
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 620
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 621
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 622
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 623
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MES A 624
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MES A 625
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 92H A 627
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 1PG A 628
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG A 629
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG A 606 bound
REMARK 800 to ASN A 57
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 800 604 through FUC A 605 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 800 609 through FUC A 611 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 608 bound
REMARK 800 to ASN A 256
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 800 601 through FUC A 603 bound to ASN A 341
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG A 607 bound
REMARK 800 to ASN A 485
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residues SO4 A 617 and 92H A
REMARK 800 626
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residues SO4 A 618 and 92H A
REMARK 800 626
DBREF 5NN0 A 1 529 UNP P06276 CHLE_HUMAN 29 557
SEQADV 5NN0 GLN A 17 UNP P06276 ASN 45 ENGINEERED MUTATION
SEQADV 5NN0 GLN A 455 UNP P06276 ASN 483 ENGINEERED MUTATION
SEQADV 5NN0 GLN A 481 UNP P06276 ASN 509 ENGINEERED MUTATION
SEQRES 1 A 529 GLU ASP ASP ILE ILE ILE ALA THR LYS ASN GLY LYS VAL
SEQRES 2 A 529 ARG GLY MET GLN 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 GLN
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 GLN
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
HET NAG A 601 14
HET NAG A 602 14
HET FUC A 603 10
HET NAG A 604 14
HET FUC A 605 10
HET NAG A 606 14
HET NAG A 607 14
HET NAG A 608 14
HET NAG A 609 14
HET NAG A 610 14
HET FUC A 611 10
HET GOL A 612 6
HET GOL A 613 6
HET SO4 A 614 5
HET SO4 A 615 5
HET SO4 A 616 5
HET SO4 A 617 5
HET SO4 A 618 5
HET SO4 A 619 5
HET SO4 A 620 5
HET CL A 621 1
HET CL A 622 1
HET CL A 623 1
HET MES A 624 12
HET MES A 625 12
HET 92H A 626 34
HET 92H A 627 34
HET 1PG A 628 17
HET PEG A 629 7
HETNAM NAG N-ACETYL-D-GLUCOSAMINE
HETNAM FUC ALPHA-L-FUCOSE
HETNAM GOL GLYCEROL
HETNAM SO4 SULFATE ION
HETNAM CL CHLORIDE ION
HETNAM MES 2-(N-MORPHOLINO)-ETHANESULFONIC ACID
HETNAM 92H ~{N}-[[(3~{R})-1-(2,3-DIHYDRO-1~{H}-INDEN-2-YL)
HETNAM 2 92H PIPERIDIN-3-YL]METHYL]-~{N}-[2-(DIMETHYLAMINO)
HETNAM 3 92H ETHYL]NAPHTHALENE-2-CARBOXAMIDE
HETNAM 1PG 2-(2-{2-[2-(2-METHOXY-ETHOXY)-ETHOXY]-ETHOXY}-ETHOXY)-
HETNAM 2 1PG ETHANOL
HETNAM PEG DI(HYDROXYETHYL)ETHER
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 2 NAG 8(C8 H15 N O6)
FORMUL 2 FUC 3(C6 H12 O5)
FORMUL 8 GOL 2(C3 H8 O3)
FORMUL 10 SO4 7(O4 S 2-)
FORMUL 17 CL 3(CL 1-)
FORMUL 20 MES 2(C6 H13 N O4 S)
FORMUL 22 92H 2(C30 H37 N3 O)
FORMUL 24 1PG C11 H24 O6
FORMUL 25 PEG C4 H10 O3
FORMUL 26 HOH *314(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 ARG A 265 1 10
HELIX 12 AB3 ASP A 268 ALA A 277 1 10
HELIX 13 AB4 MET A 302 LEU A 309 1 8
HELIX 14 AB5 GLY A 326 VAL A 331 1 6
HELIX 15 AB6 THR A 346 PHE A 358 1 13
HELIX 16 AB7 SER A 362 ASP A 375 1 14
HELIX 17 AB8 GLU A 383 PHE A 398 1 16
HELIX 18 AB9 PHE A 398 GLU A 411 1 14
HELIX 19 AC1 PRO A 431 GLY A 435 5 5
HELIX 20 AC2 GLU A 441 PHE A 446 1 6
HELIX 21 AC3 GLY A 447 GLN A 455 5 9
HELIX 22 AC4 THR A 457 GLY A 478 1 22
HELIX 23 AC5 ARG A 515 PHE A 525 1 11
HELIX 24 AC6 PHE A 526 VAL A 529 5 4
SHEET 1 AA1 3 ILE A 5 THR A 8 0
SHEET 2 AA1 3 GLY A 11 ARG A 14 -1 O VAL A 13 N ILE A 6
SHEET 3 AA1 3 ILE A 55 ASN A 57 1 O TRP A 56 N ARG A 14
SHEET 1 AA211 MET A 16 THR A 19 0
SHEET 2 AA211 THR A 24 PRO A 32 -1 O VAL A 25 N LEU A 18
SHEET 3 AA211 TYR A 94 PRO A 100 -1 O LEU A 95 N ILE A 31
SHEET 4 AA211 ILE A 140 MET A 144 -1 O SER A 143 N ASN A 96
SHEET 5 AA211 ALA A 107 ILE A 113 1 N TRP A 112 O VAL A 142
SHEET 6 AA211 GLY A 187 GLU A 197 1 O ASN A 188 N ALA A 107
SHEET 7 AA211 ARG A 219 GLN A 223 1 O GLN A 223 N GLY A 196
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
SSBOND 1 CYS A 65 CYS A 92 1555 1555 2.06
SSBOND 2 CYS A 252 CYS A 263 1555 1555 2.06
SSBOND 3 CYS A 400 CYS A 519 1555 1555 2.06
LINK ND2 ASN A 57 C1 NAG A 606 1555 1555 1.45
LINK ND2 ASN A 106 C1 NAG A 604 1555 1555 1.50
LINK ND2 ASN A 241 C1 NAG A 609 1555 1555 1.57
LINK ND2 ASN A 256 C1 NAG A 608 1555 1555 1.49
LINK ND2 ASN A 341 C1 NAG A 601 1555 1555 1.46
LINK ND2 ASN A 485 C1 NAG A 607 1555 1555 1.48
LINK O4 NAG A 601 C1 NAG A 602 1555 1555 1.43
LINK O6 NAG A 601 C1 FUC A 603 1555 1555 1.42
LINK O6 NAG A 604 C1 FUC A 605 1555 1555 1.49
LINK O4 NAG A 609 C1 NAG A 610 1555 1555 1.48
LINK O6 NAG A 609 C1 FUC A 611 1555 1555 1.26
LINK O4 SO4 A 617 CAI 92H A 626 1555 4555 1.38
LINK O2 SO4 A 618 CAM 92H A 626 1555 4555 1.38
CISPEP 1 ALA A 101 PRO A 102 0 -0.83
SITE 1 AC1 5 LEU A 18 TYR A 61 TRP A 98 ASP A 129
SITE 2 AC1 5 LYS A 131
SITE 1 AC2 3 ASN A 85 HIS A 126 1PG A 628
SITE 1 AC3 6 LEU A 208 HIS A 214 PHE A 312 LYS A 313
SITE 2 AC3 6 HOH A 759 HOH A 935
SITE 1 AC4 4 GLN A 316 GLY A 413 ASN A 414 ASN A 415
SITE 1 AC5 7 TRP A 231 ARG A 242 SER A 287 VAL A 288
SITE 2 AC5 7 HOH A 710 HOH A 716 HOH A 725
SITE 1 AC6 5 SER A 487 THR A 488 THR A 508 HOH A 706
SITE 2 AC6 5 HOH A 742
SITE 1 AC7 3 SER A 368 HIS A 372 PHE A 525
SITE 1 AC8 2 THR A 512 HOH A 951
SITE 1 AC9 1 ARG A 265
SITE 1 AD1 1 ARG A 347
SITE 1 AD2 4 HIS A 372 TYR A 373 GLN A 517 GLN A 518
SITE 1 AD3 6 LYS A 323 TYR A 420 ARG A 509 LEU A 514
SITE 2 AD3 6 ARG A 515 HOH A 914
SITE 1 AD4 14 ILE A 69 ASP A 70 TRP A 82 GLY A 116
SITE 2 AD4 14 GLY A 117 GLU A 197 SER A 198 TRP A 231
SITE 3 AD4 14 LEU A 286 PHE A 329 TYR A 332 HOH A 724
SITE 4 AD4 14 HOH A 734 HOH A 805
SITE 1 AD5 11 PHE A 76 HIS A 77 GLU A 80 MET A 81
SITE 2 AD5 11 HIS A 126 VAL A 127 LYS A 427 TYR A 440
SITE 3 AD5 11 GLU A 443 GOL A 613 HOH A 853
SITE 1 AD6 6 ARG A 219 THR A 315 GLN A 316 TYR A 477
SITE 2 AD6 6 HOH A 833 HOH A 874
SITE 1 AD7 1 ASN A 57
SITE 1 AD8 7 ASN A 106 ASN A 188 LYS A 190 SER A 191
SITE 2 AD8 7 HOH A 804 HOH A 833 HOH A 845
SITE 1 AD9 9 GLU A 238 ASN A 241 ASN A 245 LEU A 249
SITE 2 AD9 9 PHE A 278 VAL A 280 HOH A 703 HOH A 760
SITE 3 AD9 9 HOH A 836
SITE 1 AE1 1 ASN A 256
SITE 1 AE2 6 PRO A 335 GLY A 336 SER A 338 ASN A 341
SITE 2 AE2 6 HOH A 721 HOH A 775
SITE 1 AE3 4 ARG A 465 ASN A 485 SO4 A 618 HOH A 837
SITE 1 AE4 10 ARG A 135 VAL A 136 LEU A 236 TYR A 237
SITE 2 AE4 10 VAL A 294 GLY A 296 THR A 300 MET A 302
SITE 3 AE4 10 ARG A 465 SO4 A 618
SITE 1 AE5 11 ARG A 135 VAL A 136 LEU A 236 VAL A 294
SITE 2 AE5 11 GLY A 296 THR A 300 MET A 302 ARG A 465
SITE 3 AE5 11 NAG A 607 SO4 A 617 HOH A 718
CRYST1 154.970 154.970 126.680 90.00 90.00 90.00 I 4 2 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 0.006453 0.000000 0.000000 0.00000
SCALE2 0.000000 0.006453 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007894 0.00000
TER 4237 VAL A 529
MASTER 448 0 29 24 14 0 42 6 4785 1 317 41
END |