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HEADER HYDROLASE 14-OCT-17 6EQP
TITLE HUMAN BUTYRYLCHOLINESTERASE IN COMPLEX WITH ETHOPROPAZINE
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, PHENOTHIAZINE
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 6EQP 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. 2.35 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) : 2.35
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 54.88
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.348
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.5
REMARK 3 NUMBER OF REFLECTIONS : 34472
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.189
REMARK 3 R VALUE (WORKING SET) : 0.188
REMARK 3 FREE R VALUE : 0.237
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 3.002
REMARK 3 FREE R VALUE TEST SET COUNT : 1035
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 54.8970 - 4.4936 0.98 4948 154 0.1575 0.2013
REMARK 3 2 4.4936 - 3.5669 1.00 4811 148 0.1514 0.2045
REMARK 3 3 3.5669 - 3.1160 1.00 4777 148 0.1991 0.2522
REMARK 3 4 3.1160 - 2.8312 1.00 4775 148 0.2268 0.2751
REMARK 3 5 2.8312 - 2.6282 1.00 4714 146 0.2429 0.3007
REMARK 3 6 2.6282 - 2.4733 1.00 4728 146 0.2591 0.2973
REMARK 3 7 2.4733 - 2.3494 0.99 4684 145 0.2865 0.3559
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) : 0.290
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 27.034
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 45.10
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 57.56
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 4541
REMARK 3 ANGLE : 0.702 6194
REMARK 3 CHIRALITY : 0.056 682
REMARK 3 PLANARITY : 0.004 783
REMARK 3 DIHEDRAL : 10.455 3616
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): 28.3602 -22.2124 19.3351
REMARK 3 T TENSOR
REMARK 3 T11: 0.5334 T22: 0.6182
REMARK 3 T33: 0.3752 T12: 0.0973
REMARK 3 T13: 0.0555 T23: -0.1448
REMARK 3 L TENSOR
REMARK 3 L11: 1.6892 L22: 2.3130
REMARK 3 L33: 1.9818 L12: 0.3551
REMARK 3 L13: -0.0851 L23: 0.7597
REMARK 3 S TENSOR
REMARK 3 S11: 0.0293 S12: 0.5791 S13: -0.2234
REMARK 3 S21: -0.7323 S22: -0.1671 S23: -0.0117
REMARK 3 S31: 0.0525 S32: -0.1601 S33: 0.1204
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN A AND RESSEQ 66:91
REMARK 3 ORIGIN FOR THE GROUP (A): 44.7687 -24.6166 34.3841
REMARK 3 T TENSOR
REMARK 3 T11: 0.4139 T22: 0.5008
REMARK 3 T33: 0.5258 T12: 0.0774
REMARK 3 T13: 0.0810 T23: -0.0789
REMARK 3 L TENSOR
REMARK 3 L11: 0.9167 L22: 1.0547
REMARK 3 L33: 1.7624 L12: -0.5583
REMARK 3 L13: 0.6346 L23: -0.5716
REMARK 3 S TENSOR
REMARK 3 S11: 0.1113 S12: 0.3317 S13: 0.0860
REMARK 3 S21: -0.0599 S22: -0.1975 S23: -0.2911
REMARK 3 S31: -0.0431 S32: 0.5680 S33: 0.0310
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): 25.4791 -17.2119 32.8306
REMARK 3 T TENSOR
REMARK 3 T11: 0.2919 T22: 0.3630
REMARK 3 T33: 0.3174 T12: 0.0538
REMARK 3 T13: 0.0432 T23: -0.0337
REMARK 3 L TENSOR
REMARK 3 L11: 2.3337 L22: 1.9409
REMARK 3 L33: 2.1825 L12: 0.1213
REMARK 3 L13: -0.0457 L23: 0.9940
REMARK 3 S TENSOR
REMARK 3 S11: 0.1201 S12: 0.3540 S13: -0.1049
REMARK 3 S21: -0.2591 S22: -0.1047 S23: 0.0381
REMARK 3 S31: 0.0374 S32: -0.1778 S33: -0.0036
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): 24.9239 -19.3023 49.3407
REMARK 3 T TENSOR
REMARK 3 T11: 0.3421 T22: 0.3259
REMARK 3 T33: 0.3473 T12: 0.0127
REMARK 3 T13: 0.0562 T23: -0.0510
REMARK 3 L TENSOR
REMARK 3 L11: 2.2768 L22: 1.6361
REMARK 3 L33: 1.5443 L12: -0.1911
REMARK 3 L13: -0.2749 L23: 0.2746
REMARK 3 S TENSOR
REMARK 3 S11: 0.0359 S12: -0.0935 S13: -0.1766
REMARK 3 S21: 0.1733 S22: 0.0168 S23: 0.0957
REMARK 3 S31: 0.1688 S32: -0.0753 S33: -0.0791
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): 48.2715 -2.4848 30.3622
REMARK 3 T TENSOR
REMARK 3 T11: 0.5873 T22: 0.6124
REMARK 3 T33: 0.7454 T12: -0.0444
REMARK 3 T13: 0.2255 T23: 0.0491
REMARK 3 L TENSOR
REMARK 3 L11: 2.5288 L22: 1.9993
REMARK 3 L33: 3.6738 L12: 0.1325
REMARK 3 L13: -1.0797 L23: -0.6924
REMARK 3 S TENSOR
REMARK 3 S11: 0.2130 S12: 0.1979 S13: 0.3422
REMARK 3 S21: -0.2312 S22: -0.3708 S23: -0.7835
REMARK 3 S31: -1.0168 S32: 0.9380 S33: 0.0682
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): 44.8865 -13.0633 61.0710
REMARK 3 T TENSOR
REMARK 3 T11: 0.4228 T22: 0.4998
REMARK 3 T33: 0.3887 T12: 0.0558
REMARK 3 T13: -0.0029 T23: -0.1255
REMARK 3 L TENSOR
REMARK 3 L11: 2.4472 L22: 3.5511
REMARK 3 L33: 3.0578 L12: -0.5811
REMARK 3 L13: 0.5626 L23: 1.2856
REMARK 3 S TENSOR
REMARK 3 S11: -0.0314 S12: -0.2469 S13: 0.0492
REMARK 3 S21: 0.4087 S22: 0.3027 S23: -0.3100
REMARK 3 S31: 0.0267 S32: 0.4520 S33: -0.2544
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 6EQP COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 14-OCT-17.
REMARK 100 THE DEPOSITION ID IS D_1200007082.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 05-DEC-12
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 : ID23-2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.87260
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 225 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 34489
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.349
REMARK 200 RESOLUTION RANGE LOW (A) : 54.890
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.5
REMARK 200 DATA REDUNDANCY : 6.600
REMARK 200 R MERGE (I) : 0.07518
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 19.1600
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.35
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.43
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.6
REMARK 200 DATA REDUNDANCY IN SHELL : 6.60
REMARK 200 R MERGE FOR SHELL (I) : 0.88350
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 2.260
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: 1P0I
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 64.17
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.43
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 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 77.61500
REMARK 290 SMTRY2 9 0.000000 1.000000 0.000000 77.61500
REMARK 290 SMTRY3 9 0.000000 0.000000 1.000000 67.65000
REMARK 290 SMTRY1 10 -1.000000 0.000000 0.000000 77.61500
REMARK 290 SMTRY2 10 0.000000 -1.000000 0.000000 77.61500
REMARK 290 SMTRY3 10 0.000000 0.000000 1.000000 67.65000
REMARK 290 SMTRY1 11 0.000000 -1.000000 0.000000 77.61500
REMARK 290 SMTRY2 11 1.000000 0.000000 0.000000 77.61500
REMARK 290 SMTRY3 11 0.000000 0.000000 1.000000 67.65000
REMARK 290 SMTRY1 12 0.000000 1.000000 0.000000 77.61500
REMARK 290 SMTRY2 12 -1.000000 0.000000 0.000000 77.61500
REMARK 290 SMTRY3 12 0.000000 0.000000 1.000000 67.65000
REMARK 290 SMTRY1 13 -1.000000 0.000000 0.000000 77.61500
REMARK 290 SMTRY2 13 0.000000 1.000000 0.000000 77.61500
REMARK 290 SMTRY3 13 0.000000 0.000000 -1.000000 67.65000
REMARK 290 SMTRY1 14 1.000000 0.000000 0.000000 77.61500
REMARK 290 SMTRY2 14 0.000000 -1.000000 0.000000 77.61500
REMARK 290 SMTRY3 14 0.000000 0.000000 -1.000000 67.65000
REMARK 290 SMTRY1 15 0.000000 1.000000 0.000000 77.61500
REMARK 290 SMTRY2 15 1.000000 0.000000 0.000000 77.61500
REMARK 290 SMTRY3 15 0.000000 0.000000 -1.000000 67.65000
REMARK 290 SMTRY1 16 0.000000 -1.000000 0.000000 77.61500
REMARK 290 SMTRY2 16 -1.000000 0.000000 0.000000 77.61500
REMARK 290 SMTRY3 16 0.000000 0.000000 -1.000000 67.65000
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: 4120 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 21370 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -62.0 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 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 GLN A 486 CG CD OE1 NE2
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 -2.02 72.94
REMARK 500 ASP A 54 -157.88 -93.84
REMARK 500 ALA A 58 68.23 -114.86
REMARK 500 ASN A 106 60.42 -155.50
REMARK 500 ALA A 162 78.95 -155.59
REMARK 500 SER A 198 -123.41 60.50
REMARK 500 ASP A 297 -80.13 -128.04
REMARK 500 GLN A 311 79.29 -102.29
REMARK 500 ASN A 341 -168.73 -124.43
REMARK 500 PHE A 398 -53.34 -138.67
REMARK 500 ARG A 453 33.47 -88.67
REMARK 500 ARG A 453 33.47 -85.48
REMARK 500 ASN A 485 58.76 -105.69
REMARK 500 GLN A 486 41.58 39.58
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 BUW A 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 613
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 614
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 615
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 616
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 617
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 618
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 619
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 620
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 621
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG A 602 bound
REMARK 800 to ASN A 57
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG A
REMARK 800 603 through FUC A 604 bound to ASN A 106
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG A
REMARK 800 605 through NAG A 607 bound to ASN A 241
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD5
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: AD6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG A
REMARK 800 609 through NAG A 611 bound to ASN A 341
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG A 612 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
DBREF 6EQP A 1 529 UNP P06276 CHLE_HUMAN 29 557
SEQADV 6EQP GLN A 17 UNP P06276 ASN 45 ENGINEERED MUTATION
SEQADV 6EQP GLN A 455 UNP P06276 ASN 483 ENGINEERED MUTATION
SEQADV 6EQP GLN A 481 UNP P06276 ASN 509 ENGINEERED MUTATION
SEQADV 6EQP 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 BUW A 601 30
HET NAG A 602 14
HET NAG A 603 14
HET FUC A 604 10
HET NAG A 605 14
HET FUL A 606 10
HET NAG A 607 14
HET NAG A 608 14
HET NAG A 609 14
HET FUL A 610 10
HET NAG A 611 14
HET NAG A 612 14
HET CL A 613 1
HET CL A 614 1
HET CL A 615 1
HET CL A 616 1
HET CL A 617 1
HET CL A 618 1
HET CL A 619 1
HET ZN A 620 1
HET SO4 A 621 5
HETNAM BUW R-ETHOPROPAZINE
HETNAM NAG N-ACETYL-D-GLUCOSAMINE
HETNAM FUC ALPHA-L-FUCOSE
HETNAM FUL BETA-L-FUCOSE
HETNAM CL CHLORIDE ION
HETNAM ZN ZINC ION
HETNAM SO4 SULFATE ION
HETSYN FUL 6-DEOXY-BETA-L-GALACTOSE
FORMUL 2 BUW C19 H24 N2 S
FORMUL 3 NAG 8(C8 H15 N O6)
FORMUL 4 FUC C6 H12 O5
FORMUL 5 FUL 2(C6 H12 O5)
FORMUL 9 CL 7(CL 1-)
FORMUL 16 ZN ZN 2+
FORMUL 17 SO4 O4 S 2-
FORMUL 18 HOH *237(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 HIS A 214 5 4
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 GLN A 455 5 9
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 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 LYS A 12
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 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 2.04
LINK ND2 ASN A 57 C1 NAG A 602 1555 1555 1.43
LINK ND2 ASN A 106 C1 NAG A 603 1555 1555 1.44
LINK ND2 ASN A 241 C1 NAG A 605 1555 1555 1.42
LINK ND2 ASN A 256 C1 NAG A 608 1555 1555 1.43
LINK ND2 ASN A 341 C1 NAG A 609 1555 1555 1.43
LINK ND2 ASN A 485 C1 NAG A 612 1555 1555 1.42
LINK O6 NAG A 603 C1 FUC A 604 1555 1555 1.45
LINK O4 NAG A 605 C1 NAG A 607 1555 1555 1.46
LINK O6 NAG A 605 C1 FUL A 606 1555 1555 1.43
LINK O4 NAG A 609 C1 NAG A 611 1555 1555 1.44
LINK O6 NAG A 609 C1 FUL A 610 1555 1555 1.44
CISPEP 1 ALA A 101 PRO A 102 0 1.62
SITE 1 AC1 11 TRP A 82 GLY A 116 GLN A 119 THR A 120
SITE 2 AC1 11 SER A 198 TRP A 231 PRO A 285 SER A 287
SITE 3 AC1 11 PHE A 329 TYR A 332 ZN A 620
SITE 1 AC2 1 VAL A 288
SITE 1 AC3 1 ARG A 347
SITE 1 AC4 2 TYR A 420 ARG A 515
SITE 1 AC5 1 GLN A 316
SITE 1 AC6 2 PHE A 217 THR A 218
SITE 1 AC7 1 THR A 512
SITE 1 AC8 1 ARG A 515
SITE 1 AC9 1 BUW A 601
SITE 1 AD1 4 SER A 487 THR A 488 THR A 508 HOH A 777
SITE 1 AD2 2 ARG A 14 ASN A 57
SITE 1 AD3 5 ASN A 106 ASN A 188 LYS A 190 SER A 191
SITE 2 AD3 5 HOH A 701
SITE 1 AD4 5 TYR A 237 ASN A 241 ASN A 245 LEU A 249
SITE 2 AD4 5 PHE A 278
SITE 1 AD5 1 ASN A 256
SITE 1 AD6 4 GLY A 336 SER A 338 ASN A 341 HOH A 730
SITE 1 AD7 5 ARG A 465 GLU A 482 ASN A 485 HOH A 705
SITE 2 AD7 5 HOH A 726
CRYST1 155.230 155.230 135.300 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 0.006442 0.000000 0.000000 0.00000
SCALE2 0.000000 0.006442 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007391 0.00000
TER 4226 VAL A 529
MASTER 463 0 21 25 14 0 21 6 4605 1 189 41
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