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HEADER HYDROLASE 02-AUG-22 8AM1
TITLE HUMAN BUTYRYLCHOLINESTERASE IN COMPLEX WITH ZINC AND N,N,N-TRIMETHYL-
TITLE 2 2-OXO-2-(2-(PYRIDIN-2-YLMETHYLENE)HYDRAZINEYL)ETHAN-1-AMINIUM
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;
COMPND 9 OTHER_DETAILS: ENGINEERED BUTYRYLCHOLINESTERASE FOR CRYSTALLISATION
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: BCHE, CHE1;
SOURCE 6 EXPRESSION_SYSTEM: CRICETULUS GRISEUS;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 10029
KEYWDS INHIBITOR, COMPLEX, ZINC, BUTYRYLCHOLINESTERASE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR F.NACHON,X.BRAZZOLOTTO,J.DIAS
REVDAT 1 14-JUN-23 8AM1 0
JRNL AUTH F.NACHON,X.BRAZZOLOTTO,J.DIAS,C.COURAGEUX,W.DROZDZ,X.Y.CAO,
JRNL AUTH 2 A.R.STEFANKIEWICZ,J.M.LEHN
JRNL TITL GRID-TYPE QUATERNARY METALLOSUPRAMOLECULAR COMPOUNDS INHIBIT
JRNL TITL 2 HUMAN CHOLINESTERASES THROUGH DYNAMIC MULTIVALENT
JRNL TITL 3 INTERACTIONS.
JRNL REF CHEMBIOCHEM V. 23 00456 2022
JRNL REFN ESSN 1439-7633
JRNL PMID 36193860
JRNL DOI 10.1002/CBIC.202200456
REMARK 2
REMARK 2 RESOLUTION. 2.53 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.20.1_4487
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 : GEOSTD + MONOMER LIBRARY + CDL V1.2
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.53
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 109.54
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 27476
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.190
REMARK 3 R VALUE (WORKING SET) : 0.188
REMARK 3 FREE R VALUE : 0.224
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.920
REMARK 3 FREE R VALUE TEST SET COUNT : 1351
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1109.5400 - 5.4600 1.00 2800 120 0.1800 0.1912
REMARK 3 2 5.4600 - 4.3300 1.00 2630 150 0.1479 0.1762
REMARK 3 3 4.3300 - 3.7900 1.00 2620 124 0.1534 0.1795
REMARK 3 4 3.7900 - 3.4400 1.00 2619 133 0.1714 0.2230
REMARK 3 5 3.4400 - 3.1900 1.00 2601 134 0.1959 0.2741
REMARK 3 6 3.1900 - 3.0100 1.00 2588 131 0.2494 0.3065
REMARK 3 7 3.0100 - 2.8600 1.00 2556 144 0.2340 0.2862
REMARK 3 8 2.8500 - 2.7300 1.00 2569 144 0.2480 0.3112
REMARK 3 9 2.7300 - 2.6300 1.00 2554 148 0.2885 0.3323
REMARK 3 10 2.6300 - 2.5300 1.00 2588 123 0.3234 0.3768
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) : 0.363
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 27.139
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 57.87
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 70.60
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.009 4561
REMARK 3 ANGLE : 0.975 6192
REMARK 3 CHIRALITY : 0.059 676
REMARK 3 PLANARITY : 0.008 786
REMARK 3 DIHEDRAL : 10.580 658
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 3:65
REMARK 3 ORIGIN FOR THE GROUP (A): -22.3402 -28.1291 -48.3182
REMARK 3 T TENSOR
REMARK 3 T11: 0.7333 T22: 0.6698
REMARK 3 T33: 0.6036 T12: -0.1523
REMARK 3 T13: -0.1373 T23: -0.0613
REMARK 3 L TENSOR
REMARK 3 L11: 4.9424 L22: 1.6573
REMARK 3 L33: 1.4335 L12: -1.4693
REMARK 3 L13: 0.1756 L23: -0.5041
REMARK 3 S TENSOR
REMARK 3 S11: -0.0633 S12: 0.8660 S13: -0.3318
REMARK 3 S21: -0.4377 S22: 0.0618 S23: 0.2915
REMARK 3 S31: 0.0963 S32: -0.0783 S33: -0.0238
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN A AND RESSEQ 66:91
REMARK 3 ORIGIN FOR THE GROUP (A): -24.6370 -44.6208 -33.1168
REMARK 3 T TENSOR
REMARK 3 T11: 0.6684 T22: 0.6198
REMARK 3 T33: 0.8225 T12: -0.1770
REMARK 3 T13: -0.1348 T23: -0.0653
REMARK 3 L TENSOR
REMARK 3 L11: 1.7366 L22: 1.0324
REMARK 3 L33: 3.6365 L12: 0.7266
REMARK 3 L13: -1.6593 L23: -1.4577
REMARK 3 S TENSOR
REMARK 3 S11: -0.2458 S12: 0.2505 S13: -0.4564
REMARK 3 S21: -0.2769 S22: 0.3413 S23: -0.3153
REMARK 3 S31: 0.9727 S32: -0.4841 S33: -0.1519
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): -17.0781 -25.3886 -34.7770
REMARK 3 T TENSOR
REMARK 3 T11: 0.4671 T22: 0.3693
REMARK 3 T33: 0.6335 T12: -0.0736
REMARK 3 T13: -0.0390 T23: -0.0554
REMARK 3 L TENSOR
REMARK 3 L11: 1.8775 L22: 1.5668
REMARK 3 L33: 1.8692 L12: -0.5086
REMARK 3 L13: 0.7200 L23: 0.1314
REMARK 3 S TENSOR
REMARK 3 S11: -0.0270 S12: 0.2298 S13: -0.0881
REMARK 3 S21: -0.2668 S22: 0.0793 S23: 0.1205
REMARK 3 S31: -0.0404 S32: 0.0097 S33: -0.0268
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): -19.0002 -24.7481 -18.3118
REMARK 3 T TENSOR
REMARK 3 T11: 0.3966 T22: 0.4012
REMARK 3 T33: 0.5660 T12: -0.0452
REMARK 3 T13: -0.0644 T23: -0.0344
REMARK 3 L TENSOR
REMARK 3 L11: 2.5940 L22: 2.4436
REMARK 3 L33: 2.0849 L12: -0.5266
REMARK 3 L13: -0.0519 L23: -0.1144
REMARK 3 S TENSOR
REMARK 3 S11: -0.0286 S12: -0.1895 S13: -0.0140
REMARK 3 S21: 0.0570 S22: 0.1491 S23: 0.1342
REMARK 3 S31: -0.0129 S32: -0.2951 S33: -0.1444
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): -2.3920 -48.1273 -37.1513
REMARK 3 T TENSOR
REMARK 3 T11: 0.6883 T22: 0.5426
REMARK 3 T33: 0.8808 T12: -0.0062
REMARK 3 T13: -0.0116 T23: -0.1767
REMARK 3 L TENSOR
REMARK 3 L11: 5.8851 L22: 6.0810
REMARK 3 L33: 8.3769 L12: -1.1891
REMARK 3 L13: -4.1541 L23: 2.3868
REMARK 3 S TENSOR
REMARK 3 S11: -0.3633 S12: 0.2930 S13: -0.9067
REMARK 3 S21: -0.2950 S22: 0.3347 S23: -0.0498
REMARK 3 S31: 1.1996 S32: 0.6872 S33: 0.0671
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): -13.0376 -44.7369 -6.4580
REMARK 3 T TENSOR
REMARK 3 T11: 0.5423 T22: 0.4748
REMARK 3 T33: 0.6666 T12: -0.0011
REMARK 3 T13: -0.0784 T23: 0.0020
REMARK 3 L TENSOR
REMARK 3 L11: 8.4243 L22: 4.4327
REMARK 3 L33: 6.4293 L12: 0.8485
REMARK 3 L13: 2.2824 L23: -0.2233
REMARK 3 S TENSOR
REMARK 3 S11: 0.2300 S12: -0.6349 S13: -0.3155
REMARK 3 S21: 0.3445 S22: -0.0014 S23: 0.0117
REMARK 3 S31: 0.5866 S32: 0.0316 S33: -0.2204
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 8AM1 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 10-AUG-22.
REMARK 100 THE DEPOSITION ID IS D_1292124725.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 10-FEB-18
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) : 0.96770
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER X 4M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 27493
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.530
REMARK 200 RESOLUTION RANGE LOW (A) : 109.540
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 10.60
REMARK 200 R MERGE (I) : 0.09455
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 19.9400
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.53
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.62
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.9
REMARK 200 DATA REDUNDANCY IN SHELL : 11.10
REMARK 200 R MERGE FOR SHELL (I) : 1.10700
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: 1P0I
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 63.72
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.39
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: AMMONIUM SULFATE 2.1 M, 2-(N
REMARK 280 -MORPHOLINO)- ETHANESULFONIC ACID 0.1 M, PH 6.5, VAPOR DIFFUSION,
REMARK 280 HANGING DROP, TEMPERATURE 298K
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 77.45500
REMARK 290 SMTRY2 9 0.000000 1.000000 0.000000 77.45500
REMARK 290 SMTRY3 9 0.000000 0.000000 1.000000 67.48500
REMARK 290 SMTRY1 10 -1.000000 0.000000 0.000000 77.45500
REMARK 290 SMTRY2 10 0.000000 -1.000000 0.000000 77.45500
REMARK 290 SMTRY3 10 0.000000 0.000000 1.000000 67.48500
REMARK 290 SMTRY1 11 0.000000 -1.000000 0.000000 77.45500
REMARK 290 SMTRY2 11 1.000000 0.000000 0.000000 77.45500
REMARK 290 SMTRY3 11 0.000000 0.000000 1.000000 67.48500
REMARK 290 SMTRY1 12 0.000000 1.000000 0.000000 77.45500
REMARK 290 SMTRY2 12 -1.000000 0.000000 0.000000 77.45500
REMARK 290 SMTRY3 12 0.000000 0.000000 1.000000 67.48500
REMARK 290 SMTRY1 13 -1.000000 0.000000 0.000000 77.45500
REMARK 290 SMTRY2 13 0.000000 1.000000 0.000000 77.45500
REMARK 290 SMTRY3 13 0.000000 0.000000 -1.000000 67.48500
REMARK 290 SMTRY1 14 1.000000 0.000000 0.000000 77.45500
REMARK 290 SMTRY2 14 0.000000 -1.000000 0.000000 77.45500
REMARK 290 SMTRY3 14 0.000000 0.000000 -1.000000 67.48500
REMARK 290 SMTRY1 15 0.000000 1.000000 0.000000 77.45500
REMARK 290 SMTRY2 15 1.000000 0.000000 0.000000 77.45500
REMARK 290 SMTRY3 15 0.000000 0.000000 -1.000000 67.48500
REMARK 290 SMTRY1 16 0.000000 -1.000000 0.000000 77.45500
REMARK 290 SMTRY2 16 -1.000000 0.000000 0.000000 77.45500
REMARK 290 SMTRY3 16 0.000000 0.000000 -1.000000 67.48500
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 APPLY THE FOLLOWING TO CHAINS: A, B, C
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 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 OE1 GLU A 482 OG SER A 487 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 -3.34 71.35
REMARK 500 GLN A 71 14.99 -141.89
REMARK 500 PHE A 153 10.18 -140.49
REMARK 500 ALA A 162 76.06 -155.47
REMARK 500 SER A 198 -121.98 58.06
REMARK 500 SER A 253 105.57 -51.82
REMARK 500 ASP A 297 -79.87 -130.22
REMARK 500 PHE A 398 -55.41 -136.52
REMARK 500 ASN A 485 31.95 -94.35
REMARK 500 SER A 507 128.69 -172.88
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 620 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 LWL A 621 O07
REMARK 620 2 LWL A 621 N09 76.7
REMARK 620 3 LWL A 621 N16 156.3 81.3
REMARK 620 4 LWL A 622 O07 93.6 121.7 90.7
REMARK 620 5 LWL A 622 O07 92.8 122.0 91.7 1.0
REMARK 620 6 LWL A 622 N09 103.3 161.2 100.3 77.1 76.8
REMARK 620 7 LWL A 622 N09 105.6 162.8 98.0 75.4 75.1 2.9
REMARK 620 N 1 2 3 4 5 6
DBREF 8AM1 A 1 529 UNP P06276 CHLE_HUMAN 29 557
SEQADV 8AM1 GLN A 17 UNP P06276 ASN 45 ENGINEERED MUTATION
SEQADV 8AM1 GLN A 455 UNP P06276 ASN 483 ENGINEERED MUTATION
SEQADV 8AM1 GLN A 481 UNP P06276 ASN 509 ENGINEERED MUTATION
SEQADV 8AM1 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 NAG B 1 14
HET NAG B 2 14
HET FUC B 3 10
HET NAG C 1 14
HET NAG C 2 14
HET FUC C 3 10
HET NAG A 601 14
HET NAG A 602 14
HET NAG A 603 14
HET NAG A 604 14
HET NH4 A 605 1
HET GOL A 606 6
HET GOL A 607 6
HET GOL A 608 6
HET GOL A 609 6
HET CL A 610 1
HET CL A 611 1
HET CL A 612 1
HET CL A 613 1
HET CL A 614 1
HET CL A 615 1
HET CL A 616 1
HET SO4 A 617 5
HET SO4 A 618 5
HET ZN A 619 1
HET ZN A 620 1
HET LWL A 621 16
HET LWL A 622 27
HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE
HETNAM FUC ALPHA-L-FUCOPYRANOSE
HETNAM NH4 AMMONIUM ION
HETNAM GOL GLYCEROL
HETNAM CL CHLORIDE ION
HETNAM SO4 SULFATE ION
HETNAM ZN ZINC ION
HETNAM LWL N,N,N-TRIMETHYL-2-OXO-2-(2-(PYRIDIN-2-YLMETHYLENE)
HETNAM 2 LWL HYDRAZINEYL)ETHAN-1-AMINIUM
HETSYN NAG N-ACETYL-BETA-D-GLUCOSAMINE; 2-ACETAMIDO-2-DEOXY-BETA-
HETSYN 2 NAG D-GLUCOSE; 2-ACETAMIDO-2-DEOXY-D-GLUCOSE; 2-ACETAMIDO-
HETSYN 3 NAG 2-DEOXY-GLUCOSE; N-ACETYL-D-GLUCOSAMINE
HETSYN FUC ALPHA-L-FUCOSE; 6-DEOXY-ALPHA-L-GALACTOPYRANOSE; L-
HETSYN 2 FUC FUCOSE; FUCOSE
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
HETSYN LWL ~{N}-[(~{E})-PYRIDIN-2-YLMETHYLIDENEAMINO]-2-
HETSYN 2 LWL (TRIMETHYL-$L^{4}-AZANYL)ETHANAMIDE
FORMUL 2 NAG 8(C8 H15 N O6)
FORMUL 2 FUC 2(C6 H12 O5)
FORMUL 8 NH4 H4 N 1+
FORMUL 9 GOL 4(C3 H8 O3)
FORMUL 13 CL 7(CL 1-)
FORMUL 20 SO4 2(O4 S 2-)
FORMUL 22 ZN 2(ZN 2+)
FORMUL 24 LWL 2(C11 H17 N4 O 1+)
FORMUL 26 HOH *95(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 HIS A 214 5 4
HELIX 10 AB1 SER A 235 GLY A 251 1 17
HELIX 11 AB2 ASN A 256 ASN A 266 1 11
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 PHE A 525 1 11
HELIX 25 AC7 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 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 2.04
SSBOND 3 CYS A 400 CYS A 519 1555 1555 2.06
LINK ND2 ASN A 57 C1 NAG A 601 1555 1555 1.46
LINK ND2 ASN A 106 C1 NAG A 602 1555 1555 1.46
LINK ND2 ASN A 241 C1 NAG B 1 1555 1555 1.45
LINK ND2 ASN A 256 C1 NAG A 603 1555 1555 1.46
LINK ND2 ASN A 341 C1 NAG C 1 1555 1555 1.44
LINK ND2 ASN A 485 C1 NAG A 604 1555 1555 1.45
LINK O4 NAG B 1 C1 NAG B 2 1555 1555 1.46
LINK O6 NAG B 1 C1 FUC B 3 1555 1555 1.45
LINK O4 NAG C 1 C1 NAG C 2 1555 1555 1.46
LINK O6 NAG C 1 C1 FUC C 3 1555 1555 1.45
LINK ZN ZN A 620 O07 LWL A 621 1555 1555 2.34
LINK ZN ZN A 620 N09 LWL A 621 1555 1555 1.96
LINK ZN ZN A 620 N16 LWL A 621 1555 1555 2.32
LINK ZN ZN A 620 O07ALWL A 622 1555 1555 1.96
LINK ZN ZN A 620 O07BLWL A 622 1555 1555 1.97
LINK ZN ZN A 620 N09ALWL A 622 1555 1555 2.49
LINK ZN ZN A 620 N09BLWL A 622 1555 1555 2.53
CISPEP 1 ALA A 101 PRO A 102 0 -2.72
CRYST1 154.910 154.910 134.970 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 0.006455 0.000000 0.000000 0.00000
SCALE2 0.000000 0.006455 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007409 0.00000
TER 4233 VAL A 529
MASTER 401 0 28 25 14 0 0 6 4506 1 223 41
END |