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HEADER HYDROLASE 15-OCT-17 6EQQ
TITLE HUMAN BUTYRYLCHOLINESTERASE IN COMPLEX WITH HUPRINE 19
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_TAXID: 10029;
SOURCE 8 EXPRESSION_SYSTEM_CELL_LINE: CHO-K1;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PGS
KEYWDS COMPLEX, HYDROLASE, INHIBITOR, HUPRINE
EXPDTA X-RAY DIFFRACTION
AUTHOR F.NACHON,X.BRAZZOLOTTO,M.WANDHAMMER,M.TROVASLET-LEROY,T.L.ROSENBERRY,
AUTHOR 2 I.R.MACDONALD,S.DARVESH
REVDAT 1 13-DEC-17 6EQQ 0
JRNL AUTH T.L.ROSENBERRY,X.BRAZZOLOTTO,I.R.MACDONALD,M.WANDHAMMER,
JRNL AUTH 2 M.TROVASLET-LEROY,S.DARVESH,F.NACHON
JRNL TITL COMPARISON OF THE BINDING OF REVERSIBLE INHIBITORS TO HUMAN
JRNL TITL 2 BUTYRYLCHOLINESTERASE AND ACETYLCHOLINESTERASE: A
JRNL TITL 3 CRYSTALLOGRAPHIC, KINETIC AND CALORIMETRIC STUDY.
JRNL REF MOLECULES V. 22 2017
JRNL REFN ESSN 1420-3049
JRNL PMID 29186056
JRNL DOI 10.3390/MOLECULES22122098
REMARK 2
REMARK 2 RESOLUTION. 2.40 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 : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.40
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 57.13
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.344
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 31856
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.172
REMARK 3 R VALUE (WORKING SET) : 0.171
REMARK 3 FREE R VALUE : 0.196
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.001
REMARK 3 FREE R VALUE TEST SET COUNT : 1593
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 57.1442 - 5.3362 1.00 2907 153 0.1856 0.2017
REMARK 3 2 5.3362 - 4.2360 1.00 2808 147 0.1394 0.1446
REMARK 3 3 4.2360 - 3.7006 1.00 2768 147 0.1378 0.1648
REMARK 3 4 3.7006 - 3.3623 1.00 2731 144 0.1551 0.1974
REMARK 3 5 3.3623 - 3.1213 1.00 2736 143 0.1776 0.2072
REMARK 3 6 3.1213 - 2.9373 1.00 2737 144 0.1784 0.2178
REMARK 3 7 2.9373 - 2.7902 1.00 2719 143 0.1819 0.1939
REMARK 3 8 2.7902 - 2.6688 1.00 2720 144 0.2047 0.2494
REMARK 3 9 2.6688 - 2.5660 1.00 2715 143 0.2185 0.2541
REMARK 3 10 2.5660 - 2.4775 1.00 2713 142 0.2321 0.2680
REMARK 3 11 2.4775 - 2.4000 1.00 2709 143 0.2526 0.3135
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.219
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 21.481
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 46.49
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 60.38
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 : 0.003 4524
REMARK 3 ANGLE : 0.629 6158
REMARK 3 CHIRALITY : 0.046 671
REMARK 3 PLANARITY : 0.004 776
REMARK 3 DIHEDRAL : 9.754 3604
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 6
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN A AND RESSEQ 4:65
REMARK 3 ORIGIN FOR THE GROUP (A): -28.0944 22.1487 -48.1239
REMARK 3 T TENSOR
REMARK 3 T11: 0.5739 T22: 0.6186
REMARK 3 T33: 0.3828 T12: 0.0963
REMARK 3 T13: -0.0072 T23: 0.1231
REMARK 3 L TENSOR
REMARK 3 L11: 2.1474 L22: 3.5477
REMARK 3 L33: 1.4563 L12: 1.0300
REMARK 3 L13: -0.1369 L23: -0.5114
REMARK 3 S TENSOR
REMARK 3 S11: 0.0155 S12: 0.5630 S13: 0.1452
REMARK 3 S21: -0.7050 S22: -0.1011 S23: 0.0453
REMARK 3 S31: -0.1378 S32: 0.0522 S33: 0.0684
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN A AND RESSEQ 66:91
REMARK 3 ORIGIN FOR THE GROUP (A): -44.3457 24.6305 -33.0077
REMARK 3 T TENSOR
REMARK 3 T11: 0.4643 T22: 0.5148
REMARK 3 T33: 0.5658 T12: 0.1047
REMARK 3 T13: -0.0288 T23: 0.1107
REMARK 3 L TENSOR
REMARK 3 L11: 0.4256 L22: 1.3033
REMARK 3 L33: 2.1558 L12: -0.6256
REMARK 3 L13: -0.9077 L23: 1.2065
REMARK 3 S TENSOR
REMARK 3 S11: 0.1168 S12: 0.2047 S13: -0.1632
REMARK 3 S21: -0.1178 S22: -0.2010 S23: 0.1957
REMARK 3 S31: -0.2968 S32: -0.6097 S33: 0.0265
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: (CHAIN A AND RESSEQ 92:153) OR (CHAIN A AND RESSEQ
REMARK 3 164:231)
REMARK 3 ORIGIN FOR THE GROUP (A): -25.2602 17.3221 -34.6516
REMARK 3 T TENSOR
REMARK 3 T11: 0.2648 T22: 0.3196
REMARK 3 T33: 0.3072 T12: 0.0340
REMARK 3 T13: -0.0497 T23: 0.0221
REMARK 3 L TENSOR
REMARK 3 L11: 1.9735 L22: 2.0351
REMARK 3 L33: 2.0336 L12: -0.1590
REMARK 3 L13: 0.0001 L23: -0.7166
REMARK 3 S TENSOR
REMARK 3 S11: 0.1107 S12: 0.3079 S13: 0.1377
REMARK 3 S21: -0.2674 S22: -0.0031 S23: 0.0418
REMARK 3 S31: -0.0251 S32: 0.1665 S33: -0.0890
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: (CHAIN A AND RESSEQ 290:326) OR (CHAIN A AND RESSEQ
REMARK 3 397:515)
REMARK 3 ORIGIN FOR THE GROUP (A): -24.4822 19.1107 -18.1752
REMARK 3 T TENSOR
REMARK 3 T11: 0.3316 T22: 0.3186
REMARK 3 T33: 0.3655 T12: 0.0111
REMARK 3 T13: -0.0744 T23: 0.0553
REMARK 3 L TENSOR
REMARK 3 L11: 2.2186 L22: 1.8951
REMARK 3 L33: 1.4951 L12: -0.4577
REMARK 3 L13: -0.2204 L23: 0.0258
REMARK 3 S TENSOR
REMARK 3 S11: 0.0222 S12: -0.1531 S13: 0.2170
REMARK 3 S21: 0.2036 S22: 0.0530 S23: -0.0795
REMARK 3 S31: -0.1486 S32: 0.0884 S33: -0.1012
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: (CHAIN A AND RESSEQ 154:163) OR (CHAIN A AND RESSEQ
REMARK 3 232:289)
REMARK 3 ORIGIN FOR THE GROUP (A): -47.9573 2.5326 -36.9325
REMARK 3 T TENSOR
REMARK 3 T11: 0.4634 T22: 0.6039
REMARK 3 T33: 0.7100 T12: -0.0130
REMARK 3 T13: -0.1372 T23: -0.0234
REMARK 3 L TENSOR
REMARK 3 L11: 3.7916 L22: 3.9368
REMARK 3 L33: 5.6098 L12: 0.9428
REMARK 3 L13: 2.0271 L23: 2.7195
REMARK 3 S TENSOR
REMARK 3 S11: 0.1050 S12: 0.1943 S13: -0.2168
REMARK 3 S21: -0.1655 S22: -0.2732 S23: 0.7574
REMARK 3 S31: 0.6596 S32: -0.8072 S33: 0.1409
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: (CHAIN A AND RESSEQ 327:396) OR (CHAIN A AND RESSEQ
REMARK 3 516:529)
REMARK 3 ORIGIN FOR THE GROUP (A): -44.3044 13.1135 -6.4736
REMARK 3 T TENSOR
REMARK 3 T11: 0.4343 T22: 0.4578
REMARK 3 T33: 0.4036 T12: 0.0298
REMARK 3 T13: -0.0080 T23: 0.1188
REMARK 3 L TENSOR
REMARK 3 L11: 3.4017 L22: 4.9222
REMARK 3 L33: 3.2255 L12: -1.4301
REMARK 3 L13: -0.4293 L23: -0.7111
REMARK 3 S TENSOR
REMARK 3 S11: -0.1346 S12: -0.3615 S13: -0.0433
REMARK 3 S21: 0.6425 S22: 0.2648 S23: 0.3163
REMARK 3 S31: -0.0021 S32: -0.3018 S33: -0.1385
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 6EQQ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 15-OCT-17.
REMARK 100 THE DEPOSITION ID IS D_1200007085.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 31-OCT-14
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 : ID29
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.979
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS3 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 31862
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.400
REMARK 200 RESOLUTION RANGE LOW (A) : 57.130
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 9.500
REMARK 200 R MERGE (I) : 0.09373
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 17.1400
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.40
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.49
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 9.10
REMARK 200 R MERGE FOR SHELL (I) : 0.92200
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 2.210
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: 1P0I
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 63.42
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.36
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M MES BUFFER, 2.1 M AMMONIUM
REMARK 280 SULFATE, PH 6.5, 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 77.14850
REMARK 290 SMTRY2 9 0.000000 1.000000 0.000000 77.14850
REMARK 290 SMTRY3 9 0.000000 0.000000 1.000000 67.05500
REMARK 290 SMTRY1 10 -1.000000 0.000000 0.000000 77.14850
REMARK 290 SMTRY2 10 0.000000 -1.000000 0.000000 77.14850
REMARK 290 SMTRY3 10 0.000000 0.000000 1.000000 67.05500
REMARK 290 SMTRY1 11 0.000000 -1.000000 0.000000 77.14850
REMARK 290 SMTRY2 11 1.000000 0.000000 0.000000 77.14850
REMARK 290 SMTRY3 11 0.000000 0.000000 1.000000 67.05500
REMARK 290 SMTRY1 12 0.000000 1.000000 0.000000 77.14850
REMARK 290 SMTRY2 12 -1.000000 0.000000 0.000000 77.14850
REMARK 290 SMTRY3 12 0.000000 0.000000 1.000000 67.05500
REMARK 290 SMTRY1 13 -1.000000 0.000000 0.000000 77.14850
REMARK 290 SMTRY2 13 0.000000 1.000000 0.000000 77.14850
REMARK 290 SMTRY3 13 0.000000 0.000000 -1.000000 67.05500
REMARK 290 SMTRY1 14 1.000000 0.000000 0.000000 77.14850
REMARK 290 SMTRY2 14 0.000000 -1.000000 0.000000 77.14850
REMARK 290 SMTRY3 14 0.000000 0.000000 -1.000000 67.05500
REMARK 290 SMTRY1 15 0.000000 1.000000 0.000000 77.14850
REMARK 290 SMTRY2 15 1.000000 0.000000 0.000000 77.14850
REMARK 290 SMTRY3 15 0.000000 0.000000 -1.000000 67.05500
REMARK 290 SMTRY1 16 0.000000 -1.000000 0.000000 77.14850
REMARK 290 SMTRY2 16 -1.000000 0.000000 0.000000 77.14850
REMARK 290 SMTRY3 16 0.000000 0.000000 -1.000000 67.05500
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: 4680 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 21180 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 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 ASP A 3
REMARK 480
REMARK 480 ZERO OCCUPANCY ATOM
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 480 M RES C SSEQI ATOMS
REMARK 480 LYS A 262 CD CE NZ
REMARK 480 LYS A 267 CE NZ
REMARK 480 LYS A 348 CD CE NZ
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 O HOH A 703 O HOH A 879 2.06
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 -7.55 74.29
REMARK 500 CYS A 92 -1.90 -141.36
REMARK 500 ALA A 162 72.54 -155.76
REMARK 500 SER A 198 -117.06 57.70
REMARK 500 TYR A 282 63.73 -108.68
REMARK 500 ASP A 297 -70.17 -128.65
REMARK 500 PHE A 398 -57.88 -139.01
REMARK 500 GLN A 455 60.03 -101.44
REMARK 500 PRO A 480 47.33 -80.27
REMARK 500 ASN A 485 47.11 -95.65
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 H19 A 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue BR A 611
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 612
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 613
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 614
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 615
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 616
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 617
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 618
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 619
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 620
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 621
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 622
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG A 609 bound
REMARK 800 to ASN A 57
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG A 602 bound
REMARK 800 to ASN A 106
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG A
REMARK 800 607 through FUL A 608 bound to ASN A 241
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG A 610 bound
REMARK 800 to ASN A 256
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 800 603 through NAG A 605 bound to ASN A 341
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG A 606 bound
REMARK 800 to ASN A 485
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 6EP4 RELATED DB: PDB
REMARK 900 6EP4 CONTAINS THE SAME PROTEIN COMPLEXED WITH DECAMETHONIUM
REMARK 900 RELATED ID: 6EQP RELATED DB: PDB
REMARK 900 6EQP CONTAINS THE SAME PROTEIN COMPLEXED WITH ETHOPROPAZINE
DBREF 6EQQ A 1 529 UNP P06276 CHLE_HUMAN 29 557
SEQADV 6EQQ GLN A 17 UNP P06276 ASN 45 ENGINEERED MUTATION
SEQADV 6EQQ GLN A 455 UNP P06276 ASN 483 ENGINEERED MUTATION
SEQADV 6EQQ GLN A 481 UNP P06276 ASN 509 ENGINEERED MUTATION
SEQADV 6EQQ GLN A 486 UNP P06276 ASN 514 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 GLN 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 H19 A 601 22
HET NAG A 602 14
HET NAG A 603 14
HET FUL A 604 10
HET NAG A 605 14
HET NAG A 606 14
HET NAG A 607 14
HET FUL A 608 10
HET NAG A 609 14
HET NAG A 610 14
HET BR A 611 1
HET CL A 612 1
HET CL A 613 1
HET CL A 614 1
HET CL A 615 1
HET SO4 A 616 5
HET SO4 A 617 5
HET SO4 A 618 5
HET GOL A 619 6
HET GOL A 620 6
HET GOL A 621 6
HET GOL A 622 6
HET UNL A 623 6
HETNAM H19 HUPRINE 19
HETNAM NAG N-ACETYL-D-GLUCOSAMINE
HETNAM FUL BETA-L-FUCOSE
HETNAM BR BROMIDE ION
HETNAM CL CHLORIDE ION
HETNAM SO4 SULFATE ION
HETNAM GOL GLYCEROL
HETNAM UNL UNKNOWN LIGAND
HETSYN FUL 6-DEOXY-BETA-L-GALACTOSE
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 2 H19 C18 H21 CL N3 1+
FORMUL 3 NAG 7(C8 H15 N O6)
FORMUL 4 FUL 2(C6 H12 O5)
FORMUL 9 BR BR 1-
FORMUL 10 CL 4(CL 1-)
FORMUL 14 SO4 3(O4 S 2-)
FORMUL 17 GOL 4(C3 H8 O3)
FORMUL 22 HOH *209(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 LEU A 208 1 11
HELIX 9 AA9 SER A 210 PHE A 217 5 8
HELIX 10 AB1 SER A 235 GLY A 251 1 17
HELIX 11 AB2 ASN A 256 LYS A 267 1 12
HELIX 12 AB3 ASP A 268 ALA A 277 1 10
HELIX 13 AB4 PHE A 278 VAL A 280 5 3
HELIX 14 AB5 MET A 302 LEU A 309 1 8
HELIX 15 AB6 GLY A 326 VAL A 331 1 6
HELIX 16 AB7 THR A 346 PHE A 358 1 13
HELIX 17 AB8 SER A 362 TYR A 373 1 12
HELIX 18 AB9 GLU A 383 PHE A 398 1 16
HELIX 19 AC1 PHE A 398 GLU A 411 1 14
HELIX 20 AC2 PRO A 431 GLY A 435 5 5
HELIX 21 AC3 GLU A 441 PHE A 446 1 6
HELIX 22 AC4 GLY A 447 GLU A 451 5 5
HELIX 23 AC5 THR A 457 GLY A 478 1 22
HELIX 24 AC6 ARG A 515 SER A 524 1 10
HELIX 25 AC7 PHE A 525 VAL A 529 5 5
SHEET 1 AA1 3 ILE A 5 ALA A 7 0
SHEET 2 AA1 3 LYS A 12 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 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 LEU A 110 O ILE A 140
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 ILE A 221 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
SSBOND 1 CYS A 65 CYS A 92 1555 1555 2.03
SSBOND 2 CYS A 252 CYS A 263 1555 1555 2.03
SSBOND 3 CYS A 400 CYS A 519 1555 1555 2.03
LINK ND2 ASN A 57 C1 NAG A 609 1555 1555 1.44
LINK ND2 ASN A 106 C1 NAG A 602 1555 1555 1.44
LINK ND2 ASN A 241 C1 NAG A 607 1555 1555 1.45
LINK ND2 ASN A 256 C1 NAG A 610 1555 1555 1.43
LINK ND2 ASN A 341 C1 NAG A 603 1555 1555 1.44
LINK ND2 ASN A 485 C1 NAG A 606 1555 1555 1.44
LINK O4 NAG A 603 C1 NAG A 605 1555 1555 1.44
LINK O6 NAG A 603 C1 FUL A 604 1555 1555 1.44
LINK O6 NAG A 607 C1 FUL A 608 1555 1555 1.44
CISPEP 1 ALA A 101 PRO A 102 0 -0.67
SITE 1 AC1 11 ASP A 70 SER A 72 GLY A 116 GLY A 117
SITE 2 AC1 11 THR A 120 TRP A 231 LEU A 286 SER A 287
SITE 3 AC1 11 TYR A 332 PHE A 398 BR A 611
SITE 1 AC2 6 GLY A 116 GLY A 117 SER A 198 HIS A 438
SITE 2 AC2 6 H19 A 601 HOH A 774
SITE 1 AC3 1 TYR A 420
SITE 1 AC4 1 TYR A 385
SITE 1 AC5 2 ARG A 242 HOH A 890
SITE 1 AC6 2 THR A 488 THR A 508
SITE 1 AC7 4 GLN A 316 GLY A 413 ASN A 414 ASN A 415
SITE 1 AC8 2 ARG A 347 GLN A 351
SITE 1 AC9 4 ARG A 40 LYS A 262 ARG A 265 ASN A 266
SITE 1 AD1 7 LEU A 208 LEU A 209 HIS A 214 GLN A 311
SITE 2 AD1 7 PHE A 312 LYS A 313 HOH A 715
SITE 1 AD2 4 TYR A 61 TRP A 98 ASP A 129 LYS A 131
SITE 1 AD3 2 THR A 457 LYS A 458
SITE 1 AD4 4 ARG A 515 GLN A 518 HOH A 786 HOH A 831
SITE 1 AD5 2 ARG A 14 ASN A 57
SITE 1 AD6 2 ASN A 106 ASN A 188
SITE 1 AD7 4 GLU A 238 ASN A 241 ASN A 245 PHE A 278
SITE 1 AD8 1 ASN A 256
SITE 1 AD9 5 GLY A 336 SER A 338 ASN A 341 ASN A 342
SITE 2 AD9 5 HOH A 712
SITE 1 AE1 3 ARG A 465 GLU A 482 ASN A 485
CRYST1 154.297 154.297 134.110 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 0.006481 0.000000 0.000000 0.00000
SCALE2 0.000000 0.006481 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007457 0.00000
TER 4212 VAL A 529
MASTER 490 0 23 25 14 0 24 6 4594 1 191 41
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