HEADER CHAPERONE 05-DEC-16 5MKR
TITLE HSP72-NBD BOUND TO COMPOUND TCI 8 - TYR15 IN UP-CONFORMATION
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HEAT SHOCK 70 KDA PROTEIN 1A;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: UNP RESIDUES 1-380;
COMPND 5 SYNONYM: HEAT SHOCK 70 KDA PROTEIN 1,HSP70.1;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: HSPA1A, HSPA1, HSX70;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 511693
KEYWDS IRREVERSIBLE INHIBITOR, CHAPERONE, LYSINE MODIFICATION
EXPDTA X-RAY DIFFRACTION
AUTHOR J.PETTINGER,I.M.WESTWOOD,N.CRONIN,Y.-V.LE BIHAN,R.L.M.VAN MONTFORT
REVDAT 2 29-MAR-17 5MKR 1 JRNL
REVDAT 1 01-MAR-17 5MKR 0
JRNL AUTH J.PETTINGER,Y.V.LE BIHAN,M.WIDYA,R.L.VAN MONTFORT,K.JONES,
JRNL AUTH 2 M.D.CHEESEMAN
JRNL TITL AN IRREVERSIBLE INHIBITOR OF HSP72 THAT UNEXPECTEDLY TARGETS
JRNL TITL 2 LYSINE-56.
JRNL REF ANGEW. CHEM. INT. ED. ENGL. V. 56 3536 2017
JRNL REFN ESSN 1521-3773
JRNL PMID 28225177
JRNL DOI 10.1002/ANIE.201611907
REMARK 2
REMARK 2 RESOLUTION. 1.87 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : BUSTER 2.10.2
REMARK 3 AUTHORS : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER,
REMARK 3 : PACIOREK,ROVERSI,SHARFF,SMART,VONRHEIN,
REMARK 3 : WOMACK,MATTHEWS,TEN EYCK,TRONRUD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.87
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 34.98
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 94.4
REMARK 3 NUMBER OF REFLECTIONS : 35051
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING + TEST SET) : 0.167
REMARK 3 R VALUE (WORKING SET) : 0.165
REMARK 3 FREE R VALUE : 0.222
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.070
REMARK 3 FREE R VALUE TEST SET COUNT : 1777
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 18
REMARK 3 BIN RESOLUTION RANGE HIGH (ANGSTROMS) : 1.87
REMARK 3 BIN RESOLUTION RANGE LOW (ANGSTROMS) : 1.92
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 61.37
REMARK 3 REFLECTIONS IN BIN (WORKING + TEST SET) : 1830
REMARK 3 BIN R VALUE (WORKING + TEST SET) : 0.3240
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 1719
REMARK 3 BIN R VALUE (WORKING SET) : 0.3190
REMARK 3 BIN FREE R VALUE : 0.4150
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 6.07
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 111
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.000
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2954
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 47
REMARK 3 SOLVENT ATOMS : 772
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 15.62
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 18.02
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 1.37130
REMARK 3 B22 (A**2) : -1.38940
REMARK 3 B33 (A**2) : 0.01810
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.190
REMARK 3 DPI (BLOW EQ-10) BASED ON R VALUE (A) : 0.176
REMARK 3 DPI (BLOW EQ-9) BASED ON FREE R VALUE (A) : 0.156
REMARK 3 DPI (CRUICKSHANK) BASED ON R VALUE (A) : 0.139
REMARK 3 DPI (CRUICKSHANK) BASED ON FREE R VALUE (A) : 0.140
REMARK 3
REMARK 3 REFERENCES: BLOW, D. (2002) ACTA CRYST D58, 792-797
REMARK 3 CRUICKSHANK, D.W.J. (1999) ACTA CRYST D55, 583-601
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.946
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.911
REMARK 3
REMARK 3 NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15
REMARK 3 TERM COUNT WEIGHT FUNCTION.
REMARK 3 BOND LENGTHS : 3098 ; 2.000 ; HARMONIC
REMARK 3 BOND ANGLES : 4204 ; 2.000 ; HARMONIC
REMARK 3 TORSION ANGLES : 1097 ; 2.000 ; SINUSOIDAL
REMARK 3 TRIGONAL CARBON PLANES : 82 ; 2.000 ; HARMONIC
REMARK 3 GENERAL PLANES : 483 ; 5.000 ; HARMONIC
REMARK 3 ISOTROPIC THERMAL FACTORS : 3098 ; 20.000 ; HARMONIC
REMARK 3 BAD NON-BONDED CONTACTS : NULL ; NULL ; NULL
REMARK 3 IMPROPER TORSIONS : NULL ; NULL ; NULL
REMARK 3 PSEUDOROTATION ANGLES : NULL ; NULL ; NULL
REMARK 3 CHIRAL IMPROPER TORSION : 419 ; 5.000 ; SEMIHARMONIC
REMARK 3 SUM OF OCCUPANCIES : 34 ; 1.000 ; HARMONIC
REMARK 3 UTILITY DISTANCES : NULL ; NULL ; NULL
REMARK 3 UTILITY ANGLES : NULL ; NULL ; NULL
REMARK 3 UTILITY TORSION : NULL ; NULL ; NULL
REMARK 3 IDEAL-DIST CONTACT TERM : 4453 ; 4.000 ; SEMIHARMONIC
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.010
REMARK 3 BOND ANGLES (DEGREES) : 1.01
REMARK 3 PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 3.13
REMARK 3 OTHER TORSION ANGLES (DEGREES) : 15.33
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 11
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: {A|1 - 28}
REMARK 3 ORIGIN FOR THE GROUP (A): -15.3202 12.5091 -17.3099
REMARK 3 T TENSOR
REMARK 3 T11: -0.0222 T22: -0.0347
REMARK 3 T33: 0.0007 T12: -0.0108
REMARK 3 T13: 0.0149 T23: 0.0035
REMARK 3 L TENSOR
REMARK 3 L11: 2.7652 L22: 1.1213
REMARK 3 L33: 1.6421 L12: 0.7467
REMARK 3 L13: 0.1528 L23: -0.4236
REMARK 3 S TENSOR
REMARK 3 S11: 0.0127 S12: -0.0012 S13: -0.0212
REMARK 3 S21: 0.1039 S22: 0.0475 S23: 0.2554
REMARK 3 S31: 0.0372 S32: -0.1707 S33: -0.0603
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: {A|29 - 52}
REMARK 3 ORIGIN FOR THE GROUP (A): -2.3955 16.3167 -6.0591
REMARK 3 T TENSOR
REMARK 3 T11: 0.0692 T22: -0.0058
REMARK 3 T33: -0.0862 T12: 0.0061
REMARK 3 T13: 0.0005 T23: -0.0050
REMARK 3 L TENSOR
REMARK 3 L11: 1.7574 L22: 0.8796
REMARK 3 L33: 1.1553 L12: -0.4484
REMARK 3 L13: -0.0093 L23: 0.0990
REMARK 3 S TENSOR
REMARK 3 S11: 0.0083 S12: -0.2338 S13: -0.0213
REMARK 3 S21: 0.3572 S22: -0.0082 S23: 0.0407
REMARK 3 S31: 0.1862 S32: 0.0775 S33: -0.0001
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: {A|53 - 80}
REMARK 3 ORIGIN FOR THE GROUP (A): 6.5638 21.6415 -13.3657
REMARK 3 T TENSOR
REMARK 3 T11: 0.0019 T22: -0.0039
REMARK 3 T33: -0.0349 T12: 0.0026
REMARK 3 T13: -0.0312 T23: 0.0008
REMARK 3 L TENSOR
REMARK 3 L11: 1.0909 L22: 1.4307
REMARK 3 L33: 0.0000 L12: -0.3851
REMARK 3 L13: 0.4830 L23: 0.3186
REMARK 3 S TENSOR
REMARK 3 S11: -0.0412 S12: -0.0756 S13: 0.1283
REMARK 3 S21: 0.1895 S22: 0.0148 S23: -0.1517
REMARK 3 S31: -0.1253 S32: -0.1085 S33: 0.0264
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: {A|81 - 109}
REMARK 3 ORIGIN FOR THE GROUP (A): 14.1036 20.2830 -16.9180
REMARK 3 T TENSOR
REMARK 3 T11: -0.0796 T22: -0.0178
REMARK 3 T33: 0.0169 T12: -0.0069
REMARK 3 T13: -0.0066 T23: 0.0183
REMARK 3 L TENSOR
REMARK 3 L11: 1.8882 L22: 2.2909
REMARK 3 L33: 4.5895 L12: -0.1356
REMARK 3 L13: -0.8991 L23: -0.5858
REMARK 3 S TENSOR
REMARK 3 S11: 0.0637 S12: -0.0148 S13: 0.2507
REMARK 3 S21: 0.0220 S22: 0.0254 S23: -0.3598
REMARK 3 S31: -0.0721 S32: 0.2915 S33: -0.0891
REMARK 3
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: {A|110 - 151}
REMARK 3 ORIGIN FOR THE GROUP (A): -2.4669 10.6781 -16.5393
REMARK 3 T TENSOR
REMARK 3 T11: 0.0264 T22: -0.0305
REMARK 3 T33: -0.0397 T12: 0.0244
REMARK 3 T13: -0.0005 T23: 0.0079
REMARK 3 L TENSOR
REMARK 3 L11: 0.3542 L22: 0.5484
REMARK 3 L33: 0.5628 L12: 0.2434
REMARK 3 L13: -0.1816 L23: -0.1215
REMARK 3 S TENSOR
REMARK 3 S11: 0.0057 S12: -0.0655 S13: -0.0522
REMARK 3 S21: 0.0561 S22: -0.0471 S23: 0.0023
REMARK 3 S31: 0.0946 S32: 0.0820 S33: 0.0414
REMARK 3
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: {A|152 - 182}
REMARK 3 ORIGIN FOR THE GROUP (A): -4.8141 12.1926 -26.8743
REMARK 3 T TENSOR
REMARK 3 T11: 0.0232 T22: -0.0232
REMARK 3 T33: -0.0426 T12: 0.0023
REMARK 3 T13: 0.0036 T23: 0.0006
REMARK 3 L TENSOR
REMARK 3 L11: 0.0000 L22: 0.7949
REMARK 3 L33: 0.3268 L12: -0.0780
REMARK 3 L13: -0.2680 L23: -0.1463
REMARK 3 S TENSOR
REMARK 3 S11: 0.0090 S12: 0.0366 S13: -0.0148
REMARK 3 S21: -0.1319 S22: -0.0411 S23: 0.0499
REMARK 3 S31: 0.0943 S32: -0.0167 S33: 0.0320
REMARK 3
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: {A|183 - 229}
REMARK 3 ORIGIN FOR THE GROUP (A): -12.0340 26.1595 -32.4937
REMARK 3 T TENSOR
REMARK 3 T11: 0.0405 T22: -0.0508
REMARK 3 T33: -0.0785 T12: 0.0034
REMARK 3 T13: -0.0343 T23: 0.0067
REMARK 3 L TENSOR
REMARK 3 L11: 2.1905 L22: 2.1444
REMARK 3 L33: 2.1287 L12: 0.4532
REMARK 3 L13: -0.7943 L23: 0.6633
REMARK 3 S TENSOR
REMARK 3 S11: -0.0449 S12: 0.2219 S13: -0.1342
REMARK 3 S21: -0.1324 S22: 0.0883 S23: 0.1327
REMARK 3 S31: 0.2957 S32: -0.1636 S33: -0.0434
REMARK 3
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: {A|230 - 249}
REMARK 3 ORIGIN FOR THE GROUP (A): 0.6086 45.7383 -7.7689
REMARK 3 T TENSOR
REMARK 3 T11: -0.0152 T22: -0.0248
REMARK 3 T33: -0.0645 T12: -0.0010
REMARK 3 T13: 0.0066 T23: 0.0094
REMARK 3 L TENSOR
REMARK 3 L11: 1.7263 L22: 0.5002
REMARK 3 L33: 2.3492 L12: 1.4454
REMARK 3 L13: 2.5453 L23: -1.4758
REMARK 3 S TENSOR
REMARK 3 S11: 0.0299 S12: 0.0086 S13: 0.0897
REMARK 3 S21: 0.1465 S22: -0.0136 S23: -0.1922
REMARK 3 S31: -0.1209 S32: 0.1112 S33: -0.0162
REMARK 3
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: {A|250 - 292}
REMARK 3 ORIGIN FOR THE GROUP (A): -1.8271 41.6559 -1.2186
REMARK 3 T TENSOR
REMARK 3 T11: 0.0405 T22: -0.0455
REMARK 3 T33: -0.0869 T12: 0.0083
REMARK 3 T13: 0.0155 T23: 0.0113
REMARK 3 L TENSOR
REMARK 3 L11: 2.8786 L22: 1.0095
REMARK 3 L33: 4.2745 L12: -0.0214
REMARK 3 L13: 2.8963 L23: -0.2049
REMARK 3 S TENSOR
REMARK 3 S11: -0.0651 S12: 0.0023 S13: -0.0213
REMARK 3 S21: 0.1230 S22: 0.0205 S23: -0.0612
REMARK 3 S31: -0.0112 S32: 0.0877 S33: 0.0446
REMARK 3
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: {A|293 - 343}
REMARK 3 ORIGIN FOR THE GROUP (A): -9.7510 39.7903 -24.8140
REMARK 3 T TENSOR
REMARK 3 T11: -0.0140 T22: -0.0561
REMARK 3 T33: -0.0818 T12: 0.0015
REMARK 3 T13: -0.0003 T23: 0.0177
REMARK 3 L TENSOR
REMARK 3 L11: 0.5014 L22: 0.6701
REMARK 3 L33: 2.2159 L12: -0.1274
REMARK 3 L13: 0.3103 L23: 0.5529
REMARK 3 S TENSOR
REMARK 3 S11: 0.0183 S12: -0.0203 S13: 0.0049
REMARK 3 S21: -0.0531 S22: -0.0190 S23: 0.0051
REMARK 3 S31: 0.0167 S32: -0.0396 S33: 0.0006
REMARK 3
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: {A|344 - 385}
REMARK 3 ORIGIN FOR THE GROUP (A): -17.5493 26.1149 -25.7414
REMARK 3 T TENSOR
REMARK 3 T11: -0.0102 T22: 0.0029
REMARK 3 T33: 0.0037 T12: -0.0027
REMARK 3 T13: -0.0051 T23: 0.0024
REMARK 3 L TENSOR
REMARK 3 L11: 0.0951 L22: 2.1383
REMARK 3 L33: 0.3157 L12: 0.0262
REMARK 3 L13: -0.0314 L23: -0.3587
REMARK 3 S TENSOR
REMARK 3 S11: -0.0196 S12: -0.0175 S13: -0.0453
REMARK 3 S21: 0.0051 S22: 0.0334 S23: 0.1859
REMARK 3 S31: -0.0048 S32: -0.0901 S33: -0.0138
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 5MKR COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 05-DEC-16.
REMARK 100 THE DEPOSITION ID IS D_1200002119.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 27-OCT-15
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 4.1
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU FR-X
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5419
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 300K
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : AIMLESS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 35583
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.870
REMARK 200 RESOLUTION RANGE LOW (A) : 86.400
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 95.2
REMARK 200 DATA REDUNDANCY : 8.900
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 37.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.87
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.97
REMARK 200 COMPLETENESS FOR SHELL (%) : 69.4
REMARK 200 DATA REDUNDANCY IN SHELL : 2.90
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 4.800
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: IN-HOUSE
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 51.57
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.54
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 16% W/V PEG-3350, 0.06 M CITRIC ACID,
REMARK 280 0.04 M BIS-TRIS PROPANE. INHIBITOR WAS PRE-INCUBATED WITH
REMARK 280 PROTEIN PRIOR TO CO-CRYSTALLISATION., PH 4.1, VAPOR DIFFUSION,
REMARK 280 SITTING DROP, TEMPERATURE 291K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 25.33850
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 50.11600
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 43.20000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 50.11600
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 25.33850
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 43.20000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 300 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 17370 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 2.0 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 GLY A -4
REMARK 465 PRO A -3
REMARK 465 LEU A -2
REMARK 465 GLY A -1
REMARK 465 SER A 0
REMARK 465 LYS A 190
REMARK 465 ALA A 387
REMARK 465 ALA A 388
REMARK 465 SER A 389
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 MET A 1 CG SD CE
REMARK 470 LYS A 3 CE NZ
REMARK 470 GLN A 64 OE1 NE2
REMARK 470 LYS A 77 NZ
REMARK 470 LYS A 88 NZ
REMARK 470 GLN A 93 CD OE1 NE2
REMARK 470 LYS A 100 CE NZ
REMARK 470 ARG A 193 NE CZ NH1 NH2
REMARK 470 LYS A 250 CE NZ
REMARK 470 LYS A 257 CD CE NZ
REMARK 470 LYS A 319 CE NZ
REMARK 470 LYS A 325 NZ
REMARK 470 LYS A 382 NZ
REMARK 470 ALA A 386 CA C O CB
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 ASN A 62 57.31 -146.47
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 A1264 DISTANCE = 5.97 ANGSTROMS
REMARK 525 HOH A1265 DISTANCE = 5.99 ANGSTROMS
REMARK 525 HOH A1266 DISTANCE = 6.13 ANGSTROMS
REMARK 525 HOH A1267 DISTANCE = 6.15 ANGSTROMS
REMARK 525 HOH A1268 DISTANCE = 6.20 ANGSTROMS
REMARK 525 HOH A1269 DISTANCE = 6.25 ANGSTROMS
REMARK 525 HOH A1270 DISTANCE = 6.54 ANGSTROMS
REMARK 525 HOH A1271 DISTANCE = 7.32 ANGSTROMS
REMARK 525 HOH A1272 DISTANCE = 7.38 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue TI8 A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue FLC A 402
DBREF 5MKR A 1 380 UNP P0DMV8 HS71A_HUMAN 1 380
SEQADV 5MKR GLY A -4 UNP P0DMV8 EXPRESSION TAG
SEQADV 5MKR PRO A -3 UNP P0DMV8 EXPRESSION TAG
SEQADV 5MKR LEU A -2 UNP P0DMV8 EXPRESSION TAG
SEQADV 5MKR GLY A -1 UNP P0DMV8 EXPRESSION TAG
SEQADV 5MKR SER A 0 UNP P0DMV8 EXPRESSION TAG
SEQADV 5MKR ILE A 381 UNP P0DMV8 EXPRESSION TAG
SEQADV 5MKR LYS A 382 UNP P0DMV8 EXPRESSION TAG
SEQADV 5MKR SER A 383 UNP P0DMV8 EXPRESSION TAG
SEQADV 5MKR THR A 384 UNP P0DMV8 EXPRESSION TAG
SEQADV 5MKR ARG A 385 UNP P0DMV8 EXPRESSION TAG
SEQADV 5MKR ALA A 386 UNP P0DMV8 EXPRESSION TAG
SEQADV 5MKR ALA A 387 UNP P0DMV8 EXPRESSION TAG
SEQADV 5MKR ALA A 388 UNP P0DMV8 EXPRESSION TAG
SEQADV 5MKR SER A 389 UNP P0DMV8 EXPRESSION TAG
SEQRES 1 A 394 GLY PRO LEU GLY SER MET ALA LYS ALA ALA ALA ILE GLY
SEQRES 2 A 394 ILE ASP LEU GLY THR THR TYR SER CYS VAL GLY VAL PHE
SEQRES 3 A 394 GLN HIS GLY LYS VAL GLU ILE ILE ALA ASN ASP GLN GLY
SEQRES 4 A 394 ASN ARG THR THR PRO SER TYR VAL ALA PHE THR ASP THR
SEQRES 5 A 394 GLU ARG LEU ILE GLY ASP ALA ALA LYS ASN GLN VAL ALA
SEQRES 6 A 394 LEU ASN PRO GLN ASN THR VAL PHE ASP ALA LYS ARG LEU
SEQRES 7 A 394 ILE GLY ARG LYS PHE GLY ASP PRO VAL VAL GLN SER ASP
SEQRES 8 A 394 MET LYS HIS TRP PRO PHE GLN VAL ILE ASN ASP GLY ASP
SEQRES 9 A 394 LYS PRO LYS VAL GLN VAL SER TYR LYS GLY GLU THR LYS
SEQRES 10 A 394 ALA PHE TYR PRO GLU GLU ILE SER SER MET VAL LEU THR
SEQRES 11 A 394 LYS MET LYS GLU ILE ALA GLU ALA TYR LEU GLY TYR PRO
SEQRES 12 A 394 VAL THR ASN ALA VAL ILE THR VAL PRO ALA TYR PHE ASN
SEQRES 13 A 394 ASP SER GLN ARG GLN ALA THR LYS ASP ALA GLY VAL ILE
SEQRES 14 A 394 ALA GLY LEU ASN VAL LEU ARG ILE ILE ASN GLU PRO THR
SEQRES 15 A 394 ALA ALA ALA ILE ALA TYR GLY LEU ASP ARG THR GLY LYS
SEQRES 16 A 394 GLY GLU ARG ASN VAL LEU ILE PHE ASP LEU GLY GLY GLY
SEQRES 17 A 394 THR PHE ASP VAL SER ILE LEU THR ILE ASP ASP GLY ILE
SEQRES 18 A 394 PHE GLU VAL LYS ALA THR ALA GLY ASP THR HIS LEU GLY
SEQRES 19 A 394 GLY GLU ASP PHE ASP ASN ARG LEU VAL ASN HIS PHE VAL
SEQRES 20 A 394 GLU GLU PHE LYS ARG LYS HIS LYS LYS ASP ILE SER GLN
SEQRES 21 A 394 ASN LYS ARG ALA VAL ARG ARG LEU ARG THR ALA CYS GLU
SEQRES 22 A 394 ARG ALA LYS ARG THR LEU SER SER SER THR GLN ALA SER
SEQRES 23 A 394 LEU GLU ILE ASP SER LEU PHE GLU GLY ILE ASP PHE TYR
SEQRES 24 A 394 THR SER ILE THR ARG ALA ARG PHE GLU GLU LEU CYS SER
SEQRES 25 A 394 ASP LEU PHE ARG SER THR LEU GLU PRO VAL GLU LYS ALA
SEQRES 26 A 394 LEU ARG ASP ALA LYS LEU ASP LYS ALA GLN ILE HIS ASP
SEQRES 27 A 394 LEU VAL LEU VAL GLY GLY SER THR ARG ILE PRO LYS VAL
SEQRES 28 A 394 GLN LYS LEU LEU GLN ASP PHE PHE ASN GLY ARG ASP LEU
SEQRES 29 A 394 ASN LYS SER ILE ASN PRO ASP GLU ALA VAL ALA TYR GLY
SEQRES 30 A 394 ALA ALA VAL GLN ALA ALA ILE LEU ILE LYS SER THR ARG
SEQRES 31 A 394 ALA ALA ALA SER
HET TI8 A 401 34
HET FLC A 402 13
HETNAM TI8 3-[(2~{R},3~{S},4~{R},5~{R})-5-[6-AZANYL-8-[(4-
HETNAM 2 TI8 CHLOROPHENYL)METHYLAMINO]PURIN-9-YL]-3,4-
HETNAM 3 TI8 BIS(OXIDANYL)OXOLAN-2-YL]PROPYL PROP-2-ENOATE
HETNAM FLC CITRATE ANION
FORMUL 2 TI8 C22 H25 CL N6 O5
FORMUL 3 FLC C6 H5 O7 3-
FORMUL 4 HOH *772(H2 O)
HELIX 1 AA1 GLY A 52 GLN A 58 1 7
HELIX 2 AA2 VAL A 59 GLN A 64 5 6
HELIX 3 AA3 ASP A 69 ILE A 74 1 6
HELIX 4 AA4 ASP A 80 LYS A 88 1 9
HELIX 5 AA5 TYR A 115 GLY A 136 1 22
HELIX 6 AA6 ASN A 151 ALA A 165 1 15
HELIX 7 AA7 GLU A 175 TYR A 183 1 9
HELIX 8 AA8 GLY A 229 LYS A 250 1 22
HELIX 9 AA9 ASN A 256 LEU A 274 1 19
HELIX 10 AB1 ARG A 299 CYS A 306 1 8
HELIX 11 AB2 CYS A 306 SER A 312 1 7
HELIX 12 AB3 THR A 313 ALA A 324 1 12
HELIX 13 AB4 ASP A 327 ILE A 331 5 5
HELIX 14 AB5 GLY A 338 ARG A 342 5 5
HELIX 15 AB6 ILE A 343 PHE A 354 1 12
HELIX 16 AB7 GLU A 367 ARG A 385 1 19
SHEET 1 AA1 3 LYS A 25 ILE A 28 0
SHEET 2 AA1 3 TYR A 15 GLN A 22 -1 N VAL A 20 O GLU A 27
SHEET 3 AA1 3 THR A 38 PRO A 39 -1 O THR A 38 N SER A 16
SHEET 1 AA2 5 LYS A 25 ILE A 28 0
SHEET 2 AA2 5 TYR A 15 GLN A 22 -1 N VAL A 20 O GLU A 27
SHEET 3 AA2 5 ILE A 7 LEU A 11 -1 N ASP A 10 O CYS A 17
SHEET 4 AA2 5 ASN A 141 VAL A 146 1 O VAL A 143 N ILE A 9
SHEET 5 AA2 5 ASN A 168 ASN A 174 1 O LEU A 170 N ALA A 142
SHEET 1 AA3 3 ARG A 49 ILE A 51 0
SHEET 2 AA3 3 VAL A 42 PHE A 44 -1 N ALA A 43 O LEU A 50
SHEET 3 AA3 3 THR A 66 VAL A 67 -1 O VAL A 67 N VAL A 42
SHEET 1 AA4 3 GLN A 93 ASP A 97 0
SHEET 2 AA4 3 LYS A 100 TYR A 107 -1 O LYS A 102 N ILE A 95
SHEET 3 AA4 3 GLU A 110 PHE A 114 -1 O PHE A 114 N VAL A 103
SHEET 1 AA5 4 ILE A 216 ASP A 225 0
SHEET 2 AA5 4 PHE A 205 ASP A 213 -1 N ILE A 209 O LYS A 220
SHEET 3 AA5 4 GLU A 192 LEU A 200 -1 N VAL A 195 O LEU A 210
SHEET 4 AA5 4 ASP A 333 VAL A 337 1 O VAL A 335 N PHE A 198
SHEET 1 AA6 2 GLN A 279 PHE A 288 0
SHEET 2 AA6 2 ILE A 291 THR A 298 -1 O PHE A 293 N ILE A 284
SITE 1 AC1 17 THR A 37 ASP A 46 GLY A 202 GLY A 230
SITE 2 AC1 17 GLU A 268 LYS A 271 ARG A 272 SER A 275
SITE 3 AC1 17 GLY A 339 SER A 340 ARG A 342 ILE A 343
SITE 4 AC1 17 ASP A 366 HOH A 586 HOH A 656 HOH A 696
SITE 5 AC1 17 HOH A 746
SITE 1 AC2 13 ASP A 152 HIS A 240 GLU A 243 GLU A 244
SITE 2 AC2 13 ARG A 247 ARG A 301 HOH A 516 HOH A 523
SITE 3 AC2 13 HOH A 538 HOH A 616 HOH A 741 HOH A 751
SITE 4 AC2 13 HOH A 851
CRYST1 50.677 86.400 100.232 90.00 90.00 90.00 P 21 21 21 4
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 0.019733 0.000000 0.000000 0.00000
SCALE2 0.000000 0.011574 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009977 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
