HEADER CHAPERONE 22-SEP-15 5AQY
TITLE FRAGMENT-BASED SCREENING OF HSP70 SHEDS LIGHT ON THE FUNCTIONAL ROLE
TITLE 2 OF ATP-BINDING SITE RESIDUES
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HEAT SHOCK 70 KDA PROTEIN 1A;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: NUCLEOTIDE BINDING DOMAIN, UNP RESIDUES 1-380;
COMPND 5 SYNONYM: HEAT SHOCK 70 KDA PROTEIN 1, HSP70-1, HSP70.1;
COMPND 6 EC: 3.6.3.51;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE 8 EXPRESSION_SYSTEM_VARIANT: AI;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_VECTOR: PGEX-6P-1
KEYWDS HEAT SHOCK PROTEIN, HSP70, HSP72, HSC70, ATPASE, BAG1, CHAPERONE,
KEYWDS 2 FRAGMENT
EXPDTA X-RAY DIFFRACTION
AUTHOR A.M.JONES,I.M.WESTWOOD,J.D.OSBORNE,T.P.MATTHEWS,M.D.CHEESEMAN,
AUTHOR 2 M.G.ROWLANDS,F.JEGANATHAN,R.BURKE,D.LEE,N.KADI,M.LIU,M.RICHARDS,
AUTHOR 3 C.MCANDREW,N.YAHYA,S.E.DOBSON,K.JONES,P.WORKMAN,I.COLLINS,R.L.M.VAN
AUTHOR 4 MONTFORT
REVDAT 3 10-JAN-24 5AQY 1 REMARK LINK
REVDAT 2 13-SEP-17 5AQY 1 JRNL REMARK
REVDAT 1 05-OCT-16 5AQY 0
JRNL AUTH A.M.JONES,I.M.WESTWOOD,J.D.OSBORNE,T.P.MATTHEWS,
JRNL AUTH 2 M.D.CHEESEMAN,M.G.ROWLANDS,F.JEGANATHAN,R.BURKE,D.LEE,
JRNL AUTH 3 N.KADI,M.LIU,M.RICHARDS,C.MCANDREW,N.YAHYA,S.E.DOBSON,
JRNL AUTH 4 K.JONES,P.WORKMAN,I.COLLINS,R.L.VAN MONTFORT
JRNL TITL A FRAGMENT-BASED APPROACH APPLIED TO A HIGHLY FLEXIBLE
JRNL TITL 2 TARGET: INSIGHTS AND CHALLENGES TOWARDS THE INHIBITION OF
JRNL TITL 3 HSP70 ISOFORMS.
JRNL REF SCI REP V. 6 34701 2016
JRNL REFN ESSN 2045-2322
JRNL PMID 27708405
JRNL DOI 10.1038/SREP34701
REMARK 2
REMARK 2 RESOLUTION. 1.56 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) : 1.56
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 47.97
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.8
REMARK 3 NUMBER OF REFLECTIONS : 58071
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) : 0.175
REMARK 3 R VALUE (WORKING SET) : 0.174
REMARK 3 FREE R VALUE : 0.204
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.940
REMARK 3 FREE R VALUE TEST SET COUNT : 2866
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 : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (ANGSTROMS) : 1.56
REMARK 3 BIN RESOLUTION RANGE LOW (ANGSTROMS) : 1.60
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 97.48
REMARK 3 REFLECTIONS IN BIN (WORKING + TEST SET) : 4190
REMARK 3 BIN R VALUE (WORKING + TEST SET) : 0.2443
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 3973
REMARK 3 BIN R VALUE (WORKING SET) : 0.2444
REMARK 3 BIN FREE R VALUE : 0.2427
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5.18
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 217
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2962
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 108
REMARK 3 SOLVENT ATOMS : 321
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 20.90
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 28.08
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 2.35950
REMARK 3 B22 (A**2) : -5.16640
REMARK 3 B33 (A**2) : 2.80700
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) : 0.205
REMARK 3 DPI (BLOW EQ-10) BASED ON R VALUE (A) : 0.079
REMARK 3 DPI (BLOW EQ-9) BASED ON FREE R VALUE (A) : 0.080
REMARK 3 DPI (CRUICKSHANK) BASED ON R VALUE (A) : 0.076
REMARK 3 DPI (CRUICKSHANK) BASED ON FREE R VALUE (A) : 0.077
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 : 0.958
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.948
REMARK 3
REMARK 3 NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15
REMARK 3 TERM COUNT WEIGHT FUNCTION.
REMARK 3 BOND LENGTHS : 3130 ; 2.000 ; HARMONIC
REMARK 3 BOND ANGLES : 4201 ; 2.000 ; HARMONIC
REMARK 3 TORSION ANGLES : 1098 ; 2.000 ; SINUSOIDAL
REMARK 3 TRIGONAL CARBON PLANES : 80 ; 2.000 ; HARMONIC
REMARK 3 GENERAL PLANES : 467 ; 5.000 ; HARMONIC
REMARK 3 ISOTROPIC THERMAL FACTORS : 3130 ; 20.000 ; HARMONIC
REMARK 3 BAD NON-BONDED CONTACTS : 0 ; 5.000 ; SEMIHARMONIC
REMARK 3 IMPROPER TORSIONS : NULL ; NULL ; NULL
REMARK 3 PSEUDOROTATION ANGLES : NULL ; NULL ; NULL
REMARK 3 CHIRAL IMPROPER TORSION : 420 ; 5.000 ; SEMIHARMONIC
REMARK 3 SUM OF OCCUPANCIES : 4 ; 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 : 3875 ; 4.000 ; SEMIHARMONIC
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.010
REMARK 3 BOND ANGLES (DEGREES) : 0.97
REMARK 3 PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 3.41
REMARK 3 OTHER TORSION ANGLES (DEGREES) : 14.57
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 11
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: NULL
REMARK 3 ORIGIN FOR THE GROUP (A): 16.9263 -8.0895 9.8163
REMARK 3 T TENSOR
REMARK 3 T11: -0.0369 T22: 0.0195
REMARK 3 T33: -0.0409 T12: 0.0044
REMARK 3 T13: -0.0210 T23: -0.0086
REMARK 3 L TENSOR
REMARK 3 L11: 2.7494 L22: 3.7887
REMARK 3 L33: 1.4396 L12: -1.2835
REMARK 3 L13: 0.0968 L23: -0.2415
REMARK 3 S TENSOR
REMARK 3 S11: 0.0184 S12: -0.0960 S13: -0.1545
REMARK 3 S21: 0.1424 S22: 0.0039 S23: -0.1809
REMARK 3 S31: -0.0264 S32: 0.2882 S33: -0.0223
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: NULL
REMARK 3 ORIGIN FOR THE GROUP (A): -1.0277 -10.9776 -1.4796
REMARK 3 T TENSOR
REMARK 3 T11: -0.0128 T22: -0.0063
REMARK 3 T33: 0.0083 T12: -0.0032
REMARK 3 T13: -0.0092 T23: -0.0354
REMARK 3 L TENSOR
REMARK 3 L11: 1.8138 L22: 0.2319
REMARK 3 L33: 0.3244 L12: 0.1046
REMARK 3 L13: -0.5278 L23: -0.0631
REMARK 3 S TENSOR
REMARK 3 S11: 0.0298 S12: 0.1390 S13: -0.0245
REMARK 3 S21: 0.0004 S22: 0.0387 S23: -0.0459
REMARK 3 S31: 0.0728 S32: -0.0676 S33: -0.0685
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: NULL
REMARK 3 ORIGIN FOR THE GROUP (A): -11.4744 -7.0432 0.7913
REMARK 3 T TENSOR
REMARK 3 T11: -0.0621 T22: -0.0117
REMARK 3 T33: -0.0044 T12: 0.0029
REMARK 3 T13: 0.0051 T23: -0.0281
REMARK 3 L TENSOR
REMARK 3 L11: 1.3948 L22: 1.8540
REMARK 3 L33: 0.5657 L12: -0.3895
REMARK 3 L13: 0.3314 L23: 0.3398
REMARK 3 S TENSOR
REMARK 3 S11: 0.1044 S12: 0.0452 S13: 0.1075
REMARK 3 S21: -0.0713 S22: -0.0422 S23: 0.1599
REMARK 3 S31: 0.0207 S32: -0.0837 S33: -0.0622
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: NULL
REMARK 3 ORIGIN FOR THE GROUP (A): 4.3041 -7.7962 9.7838
REMARK 3 T TENSOR
REMARK 3 T11: -0.0148 T22: -0.0268
REMARK 3 T33: -0.0139 T12: 0.0025
REMARK 3 T13: -0.0145 T23: -0.0183
REMARK 3 L TENSOR
REMARK 3 L11: 1.2363 L22: 0.0303
REMARK 3 L33: 0.7535 L12: 0.2005
REMARK 3 L13: -0.0471 L23: 0.1446
REMARK 3 S TENSOR
REMARK 3 S11: 0.0387 S12: -0.0002 S13: -0.0804
REMARK 3 S21: 0.0811 S22: -0.0079 S23: 0.1367
REMARK 3 S31: 0.0972 S32: -0.0135 S33: -0.0308
REMARK 3
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: NULL
REMARK 3 ORIGIN FOR THE GROUP (A): 7.9096 1.9945 9.8949
REMARK 3 T TENSOR
REMARK 3 T11: -0.0001 T22: -0.0069
REMARK 3 T33: -0.0044 T12: -0.0009
REMARK 3 T13: 0.0046 T23: -0.0244
REMARK 3 L TENSOR
REMARK 3 L11: 1.4770 L22: 0.6702
REMARK 3 L33: 0.6343 L12: 0.6513
REMARK 3 L13: 0.0337 L23: 0.0190
REMARK 3 S TENSOR
REMARK 3 S11: 0.0994 S12: -0.1420 S13: 0.1649
REMARK 3 S21: 0.0763 S22: -0.0829 S23: 0.0953
REMARK 3 S31: -0.1007 S32: 0.0137 S33: -0.0166
REMARK 3
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: NULL
REMARK 3 ORIGIN FOR THE GROUP (A): 18.5791 8.1231 -1.8037
REMARK 3 T TENSOR
REMARK 3 T11: -0.0291 T22: -0.0210
REMARK 3 T33: -0.0264 T12: -0.0209
REMARK 3 T13: -0.0078 T23: -0.0055
REMARK 3 L TENSOR
REMARK 3 L11: 1.6280 L22: 1.1150
REMARK 3 L33: 3.2152 L12: 0.2978
REMARK 3 L13: 0.8833 L23: 1.0068
REMARK 3 S TENSOR
REMARK 3 S11: -0.0627 S12: 0.0081 S13: 0.2782
REMARK 3 S21: -0.0061 S22: 0.0686 S23: -0.0946
REMARK 3 S31: -0.2891 S32: 0.0149 S33: -0.0059
REMARK 3
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: NULL
REMARK 3 ORIGIN FOR THE GROUP (A): 6.5362 -13.9849 -25.5663
REMARK 3 T TENSOR
REMARK 3 T11: 0.1620 T22: 0.0049
REMARK 3 T33: -0.1181 T12: -0.1331
REMARK 3 T13: -0.0777 T23: 0.0471
REMARK 3 L TENSOR
REMARK 3 L11: 0.4556 L22: 3.3884
REMARK 3 L33: 0.0345 L12: 0.8209
REMARK 3 L13: -0.6785 L23: 0.4447
REMARK 3 S TENSOR
REMARK 3 S11: 0.0005 S12: -0.0673 S13: -0.1103
REMARK 3 S21: -0.1615 S22: 0.0842 S23: -0.0289
REMARK 3 S31: 0.5442 S32: -0.1974 S33: -0.0847
REMARK 3
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: NULL
REMARK 3 ORIGIN FOR THE GROUP (A): 7.4504 -20.9226 -20.9631
REMARK 3 T TENSOR
REMARK 3 T11: 0.2308 T22: -0.0917
REMARK 3 T33: -0.1850 T12: -0.1037
REMARK 3 T13: -0.0242 T23: 0.0158
REMARK 3 L TENSOR
REMARK 3 L11: 3.1879 L22: 2.6140
REMARK 3 L33: 1.6607 L12: 1.8255
REMARK 3 L13: 0.6909 L23: 1.7371
REMARK 3 S TENSOR
REMARK 3 S11: -0.1470 S12: 0.0089 S13: -0.2321
REMARK 3 S21: 0.2299 S22: 0.0956 S23: -0.1915
REMARK 3 S31: 0.5442 S32: -0.2344 S33: 0.0514
REMARK 3
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: NULL
REMARK 3 ORIGIN FOR THE GROUP (A): 15.0813 -1.3981 -20.6005
REMARK 3 T TENSOR
REMARK 3 T11: -0.0690 T22: -0.0236
REMARK 3 T33: -0.1182 T12: -0.0107
REMARK 3 T13: 0.0008 T23: 0.0318
REMARK 3 L TENSOR
REMARK 3 L11: 1.4221 L22: 2.4041
REMARK 3 L33: 5.6230 L12: 0.9482
REMARK 3 L13: 1.3245 L23: 2.9104
REMARK 3 S TENSOR
REMARK 3 S11: 0.0739 S12: 0.1963 S13: -0.1339
REMARK 3 S21: -0.0884 S22: 0.1026 S23: -0.1861
REMARK 3 S31: 0.1916 S32: 0.0391 S33: -0.1765
REMARK 3
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: NULL
REMARK 3 ORIGIN FOR THE GROUP (A): 23.8739 3.3593 -10.2298
REMARK 3 T TENSOR
REMARK 3 T11: -0.1125 T22: 0.0627
REMARK 3 T33: -0.0545 T12: 0.0103
REMARK 3 T13: -0.0015 T23: -0.0039
REMARK 3 L TENSOR
REMARK 3 L11: 1.1383 L22: 1.6333
REMARK 3 L33: 4.8080 L12: -0.4749
REMARK 3 L13: -0.0779 L23: 1.0370
REMARK 3 S TENSOR
REMARK 3 S11: 0.0634 S12: 0.2390 S13: 0.1825
REMARK 3 S21: -0.1039 S22: 0.1383 S23: -0.2565
REMARK 3 S31: -0.1231 S32: 0.4779 S33: -0.2017
REMARK 3
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: NULL
REMARK 3 ORIGIN FOR THE GROUP (A): 21.2141 0.6410 17.3517
REMARK 3 T TENSOR
REMARK 3 T11: -0.0254 T22: 0.0352
REMARK 3 T33: -0.0313 T12: -0.0282
REMARK 3 T13: -0.0417 T23: -0.0246
REMARK 3 L TENSOR
REMARK 3 L11: 1.9222 L22: 1.2004
REMARK 3 L33: 2.5960 L12: 0.2327
REMARK 3 L13: 0.7542 L23: -0.9561
REMARK 3 S TENSOR
REMARK 3 S11: 0.0740 S12: -0.3046 S13: 0.0317
REMARK 3 S21: 0.2235 S22: -0.0666 S23: -0.2736
REMARK 3 S31: -0.1349 S32: 0.1955 S33: -0.0074
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 5AQY COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 22-SEP-15.
REMARK 100 THE DEPOSITION ID IS D_1290065092.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 17-DEC-08
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : DIAMOND
REMARK 200 BEAMLINE : I02
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9728
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : AIMLESS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 58145
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.560
REMARK 200 RESOLUTION RANGE LOW (A) : 47.970
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.9
REMARK 200 DATA REDUNDANCY : 4.900
REMARK 200 R MERGE (I) : 0.08000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 5.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.56
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.59
REMARK 200 COMPLETENESS FOR SHELL (%) : 97.0
REMARK 200 DATA REDUNDANCY IN SHELL : 3.70
REMARK 200 R MERGE FOR SHELL (I) : 1.30000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.000
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: PDB ENTRY 1S3X
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 48.80
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.40
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 17-28% (W/V) PEG3350, 0.1M HEPES PH
REMARK 280 7.5, 2MM MGCL2, 2MM NAH2PO4 AND 5MM ADENOSINE
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 23.76050
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 47.97200
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 44.52300
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 47.97200
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 23.76050
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 44.52300
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 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 MET A 1
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 LYS A 25 CE NZ
REMARK 470 LYS A 190 CG CD CE NZ
REMARK 470 LYS A 246 CE NZ
REMARK 470 LYS A 248 CD CE NZ
REMARK 470 LYS A 250 CD CE NZ
REMARK 470 LYS A 257 CD CE NZ
REMARK 470 GLN A 279 CG CD OE1 NE2
REMARK 470 GLU A 315 CD OE1 OE2
REMARK 470 LYS A 325 CE NZ
REMARK 470 LYS A 348 CD CE NZ
REMARK 470 LYS A 382 CD CE NZ
REMARK 470 THR A 384 OG1 CG2
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 LYS A 361 22.80 -145.65
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 MG A1412 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH A2006 O
REMARK 620 2 HOH A2009 O 87.8
REMARK 620 3 HOH A2189 O 78.2 65.2
REMARK 620 4 HOH A2206 O 160.6 77.7 84.0
REMARK 620 N 1 2 3
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADN A 1389
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 1390
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 1391
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 1392
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 1393
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 1394
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 1395
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 1396
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 1397
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 1398
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 1399
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 1400
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 1401
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 1402
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 1403
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 1404
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 1405
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 1406
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 1407
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 1408
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 1409
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 1410
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS A 1411
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1412
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5AQF RELATED DB: PDB
REMARK 900 FRAGMENT-BASED SCREENING OF HSP70 SHEDS LIGHT ON THE FUNCTIONAL
REMARK 900 ROLE OF ATP-BINDING SITE RESIDUES
REMARK 900 RELATED ID: 5AQG RELATED DB: PDB
REMARK 900 FRAGMENT-BASED SCREENING OF HSP70 SHEDS LIGHT ON THE FUNCTIONAL
REMARK 900 ROLE OF ATP-BINDING SITE RESIDUES
REMARK 900 RELATED ID: 5AQH RELATED DB: PDB
REMARK 900 FRAGMENT-BASED SCREENING OF HSP70 SHEDS LIGHT ON THE FUNCTIONAL
REMARK 900 ROLE OF ATP-BINDING SITE RESIDUES
REMARK 900 RELATED ID: 5AQI RELATED DB: PDB
REMARK 900 FRAGMENT-BASED SCREENING OF HSP70 SHEDS LIGHT ON THE FUNCTIONAL
REMARK 900 ROLE OF ATP-BINDING SITE RESIDUES
REMARK 900 RELATED ID: 5AQJ RELATED DB: PDB
REMARK 900 FRAGMENT-BASED SCREENING OF HSP70 SHEDS LIGHT ON THE FUNCTIONAL
REMARK 900 ROLE OF ATP-BINDING SITE RESIDUES
REMARK 900 RELATED ID: 5AQK RELATED DB: PDB
REMARK 900 FRAGMENT-BASED SCREENING OF HSP70 SHEDS LIGHT ON THE FUNCTIONAL
REMARK 900 ROLE OF ATP-BINDING SITE RESIDUES
REMARK 900 RELATED ID: 5AQL RELATED DB: PDB
REMARK 900 FRAGMENT-BASED SCREENING OF HSP70 SHEDS LIGHT ON THE FUNCTIONAL
REMARK 900 ROLE OF ATP-BINDING SITE RESIDUES
REMARK 900 RELATED ID: 5AQM RELATED DB: PDB
REMARK 900 FRAGMENT-BASED SCREENING OF HSP70 SHEDS LIGHT ON THE FUNCTIONAL
REMARK 900 ROLE OF ATP-BINDING SITE RESIDUES
REMARK 900 RELATED ID: 5AQN RELATED DB: PDB
REMARK 900 FRAGMENT-BASED SCREENING OF HSP70 SHEDS LIGHT ON THE FUNCTIONAL
REMARK 900 ROLE OF ATP-BINDING SITE RESIDUES
REMARK 900 RELATED ID: 5AQO RELATED DB: PDB
REMARK 900 FRAGMENT-BASED SCREENING OF HSP70 SHEDS LIGHT ON THE FUNCTIONAL
REMARK 900 ROLE OF ATP-BINDING SITE RESIDUES
REMARK 900 RELATED ID: 5AQP RELATED DB: PDB
REMARK 900 FRAGMENT-BASED SCREENING OF HSP70 SHEDS LIGHT ON THE FUNCTIONAL
REMARK 900 ROLE OF ATP-BINDING SITE RESIDUES
REMARK 900 RELATED ID: 5AQQ RELATED DB: PDB
REMARK 900 FRAGMENT-BASED SCREENING OF HSP70 SHEDS LIGHT ON THE FUNCTIONAL
REMARK 900 ROLE OF ATP-BINDING SITE RESIDUES
REMARK 900 RELATED ID: 5AQR RELATED DB: PDB
REMARK 900 FRAGMENT-BASED SCREENING OF HSP70 SHEDS LIGHT ON THE FUNCTIONAL
REMARK 900 ROLE OF ATP-BINDING SITE RESIDUES
REMARK 900 RELATED ID: 5AQS RELATED DB: PDB
REMARK 900 FRAGMENT-BASED SCREENING OF HSP70 SHEDS LIGHT ON THE FUNCTIONAL
REMARK 900 ROLE OF ATP-BINDING SITE RESIDUES
REMARK 900 RELATED ID: 5AQT RELATED DB: PDB
REMARK 900 FRAGMENT-BASED SCREENING OF HSP70 SHEDS LIGHT ON THE FUNCTIONAL
REMARK 900 ROLE OF ATP-BINDING SITE RESIDUES
REMARK 900 RELATED ID: 5AQU RELATED DB: PDB
REMARK 900 FRAGMENT-BASED SCREENING OF HSP70 SHEDS LIGHT ON THE FUNCTIONAL
REMARK 900 ROLE OF ATP-BINDING SITE RESIDUES
REMARK 900 RELATED ID: 5AQV RELATED DB: PDB
REMARK 900 FRAGMENT-BASED SCREENING OF HSP70 SHEDS LIGHT ON THE FUNCTIONAL
REMARK 900 ROLE OF ATP-BINDING SITE RESIDUES
REMARK 900 RELATED ID: 5AQW RELATED DB: PDB
REMARK 900 FRAGMENT-BASED SCREENING OF HSP70 SHEDS LIGHT ON THE FUNCTIONAL
REMARK 900 ROLE OF ATP-BINDING SITE RESIDUES
REMARK 900 RELATED ID: 5AQX RELATED DB: PDB
REMARK 900 FRAGMENT-BASED SCREENING OF HSP70 SHEDS LIGHT ON THE FUNCTIONAL
REMARK 900 ROLE OF ATP-BINDING SITE RESIDUES
REMARK 900 RELATED ID: 5AQZ RELATED DB: PDB
REMARK 900 HSP72 WITH ADENOSINE-DERIVED INHIBITOR
REMARK 900 RELATED ID: 5AR0 RELATED DB: PDB
REMARK 900 HSP72 WITH ADENOSINE-DERIVED INHIBITOR
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 RESIDUES 382 ONWARDS ARE A CLONING ARTEFACT DERIVED FROM
REMARK 999 THE EXPRESSION VECTOR PGEX-6P-1
DBREF 5AQY A 1 380 UNP P0DMV8 HS71A_HUMAN 1 380
SEQADV 5AQY GLY A -4 UNP P0DMV8 EXPRESSION TAG
SEQADV 5AQY PRO A -3 UNP P0DMV8 EXPRESSION TAG
SEQADV 5AQY LEU A -2 UNP P0DMV8 EXPRESSION TAG
SEQADV 5AQY GLY A -1 UNP P0DMV8 EXPRESSION TAG
SEQADV 5AQY SER A 0 UNP P0DMV8 EXPRESSION TAG
SEQADV 5AQY ILE A 381 UNP P0DMV8 EXPRESSION TAG
SEQADV 5AQY LYS A 382 UNP P0DMV8 EXPRESSION TAG
SEQADV 5AQY SER A 383 UNP P0DMV8 EXPRESSION TAG
SEQADV 5AQY THR A 384 UNP P0DMV8 EXPRESSION TAG
SEQADV 5AQY ARG A 385 UNP P0DMV8 EXPRESSION TAG
SEQADV 5AQY ALA A 386 UNP P0DMV8 EXPRESSION TAG
SEQADV 5AQY ALA A 387 UNP P0DMV8 EXPRESSION TAG
SEQADV 5AQY ALA A 388 UNP P0DMV8 EXPRESSION TAG
SEQADV 5AQY 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 ADN A1389 19
HET EDO A1390 4
HET EDO A1391 4
HET EDO A1392 4
HET EDO A1393 4
HET EDO A1394 4
HET EDO A1395 4
HET EDO A1396 4
HET EDO A1397 4
HET EDO A1398 4
HET EDO A1399 4
HET EDO A1400 4
HET EDO A1401 4
HET EDO A1402 4
HET EDO A1403 4
HET EDO A1404 4
HET EDO A1405 4
HET EDO A1406 4
HET EDO A1407 4
HET EDO A1408 4
HET EDO A1409 4
HET EDO A1410 4
HET DMS A1411 4
HET MG A1412 1
HETNAM ADN ADENOSINE
HETNAM EDO 1,2-ETHANEDIOL
HETNAM DMS DIMETHYL SULFOXIDE
HETNAM MG MAGNESIUM ION
HETSYN EDO ETHYLENE GLYCOL
FORMUL 2 ADN C10 H13 N5 O4
FORMUL 3 EDO 21(C2 H6 O2)
FORMUL 24 DMS C2 H6 O S
FORMUL 25 MG MG 2+
FORMUL 26 HOH *321(H2 O)
HELIX 1 1 GLY A 52 ASN A 57 1 6
HELIX 2 2 ASN A 62 GLN A 64 5 3
HELIX 3 3 ASP A 69 LEU A 73 5 5
HELIX 4 4 ASP A 80 LYS A 88 1 9
HELIX 5 5 TYR A 115 GLY A 136 1 22
HELIX 6 6 ASN A 151 ALA A 165 1 15
HELIX 7 7 GLU A 175 TYR A 183 1 9
HELIX 8 8 GLY A 184 THR A 188 5 5
HELIX 9 9 GLY A 229 LYS A 250 1 22
HELIX 10 10 ASN A 256 LEU A 274 1 19
HELIX 11 11 ARG A 299 LYS A 325 1 27
HELIX 12 12 ASP A 327 ILE A 331 5 5
HELIX 13 13 GLY A 338 ARG A 342 5 5
HELIX 14 14 ILE A 343 PHE A 354 1 12
HELIX 15 15 GLU A 367 ILE A 381 1 15
SHEET 1 AA 2 LYS A 25 ILE A 28 0
SHEET 2 AA 2 TYR A 15 GLN A 22 1 O VAL A 20 N GLU A 27
SHEET 1 AB 2 THR A 38 PRO A 39 0
SHEET 2 AB 2 TYR A 15 GLN A 22 -1 O SER A 16 N THR A 38
SHEET 1 AC 5 ASN A 168 ASN A 174 0
SHEET 2 AC 5 ASN A 141 VAL A 146 1 O ALA A 142 N LEU A 170
SHEET 3 AC 5 ILE A 7 ASP A 10 1 O ILE A 7 N VAL A 143
SHEET 4 AC 5 TYR A 15 GLN A 22 -1 O CYS A 17 N ASP A 10
SHEET 5 AC 5 LYS A 25 ILE A 28 1 O LYS A 25 N GLN A 22
SHEET 1 AD 5 ASN A 168 ASN A 174 0
SHEET 2 AD 5 ASN A 141 VAL A 146 1 O ALA A 142 N LEU A 170
SHEET 3 AD 5 ILE A 7 ASP A 10 1 O ILE A 7 N VAL A 143
SHEET 4 AD 5 TYR A 15 GLN A 22 -1 O CYS A 17 N ASP A 10
SHEET 5 AD 5 THR A 38 PRO A 39 -1 O THR A 38 N SER A 16
SHEET 1 AE 3 ARG A 49 ILE A 51 0
SHEET 2 AE 3 VAL A 42 PHE A 44 -1 O ALA A 43 N LEU A 50
SHEET 3 AE 3 THR A 66 VAL A 67 -1 O VAL A 67 N VAL A 42
SHEET 1 AF 3 GLN A 93 ASP A 97 0
SHEET 2 AF 3 LYS A 100 TYR A 107 -1 O LYS A 100 N ASP A 97
SHEET 3 AF 3 GLU A 110 PHE A 114 -1 O GLU A 110 N TYR A 107
SHEET 1 AG 4 ILE A 216 ASP A 225 0
SHEET 2 AG 4 PHE A 205 ASP A 213 -1 O PHE A 205 N ASP A 225
SHEET 3 AG 4 ARG A 193 LEU A 200 -1 O ARG A 193 N ILE A 212
SHEET 4 AG 4 ASP A 333 VAL A 337 1 O ASP A 333 N LEU A 196
SHEET 1 AH 2 GLN A 279 PHE A 288 0
SHEET 2 AH 2 ILE A 291 THR A 298 -1 O ILE A 291 N LEU A 287
LINK MG MG A1412 O HOH A2006 1555 1555 1.97
LINK MG MG A1412 O HOH A2009 1555 1555 2.95
LINK MG MG A1412 O HOH A2189 1555 1555 2.40
LINK MG MG A1412 O HOH A2206 1555 1555 2.44
SITE 1 AC1 13 GLY A 202 GLY A 230 GLU A 268 LYS A 271
SITE 2 AC1 13 ARG A 272 SER A 275 GLY A 339 SER A 340
SITE 3 AC1 13 ARG A 342 ILE A 343 HOH A2228 HOH A2253
SITE 4 AC1 13 HOH A2314
SITE 1 AC2 7 THR A 13 LYS A 71 ARG A 72 ARG A 76
SITE 2 AC2 7 TYR A 149 PHE A 150 EDO A1397
SITE 1 AC3 10 GLY A 12 THR A 13 LYS A 71 PRO A 147
SITE 2 AC3 10 GLU A 175 THR A 204 EDO A1408 MG A1412
SITE 3 AC3 10 HOH A2006 HOH A2169
SITE 1 AC4 7 GLY A 34 ASN A 35 ARG A 36 THR A 45
SITE 2 AC4 7 THR A 47 GLU A 48 HOH A2054
SITE 1 AC5 5 ALA A 148 ARG A 155 ASN A 174 VAL A 219
SITE 2 AC5 5 EDO A1401
SITE 1 AC6 5 ARG A 49 LEU A 50 ILE A 51 LYS A 126
SITE 2 AC6 5 HOH A2320
SITE 1 AC7 4 ASP A 152 GLN A 156 LYS A 159 HOH A2178
SITE 1 AC8 6 ASN A 31 ASP A 32 THR A 38 ASP A 53
SITE 2 AC8 6 LYS A 126 EDO A1398
SITE 1 AC9 7 ARG A 72 ARG A 76 VAL A 82 ASP A 86
SITE 2 AC9 7 THR A 226 HIS A 227 EDO A1390
SITE 1 BC1 6 ASN A 31 ASP A 32 LYS A 126 ILE A 130
SITE 2 BC1 6 EDO A1396 HOH A2152
SITE 1 BC2 5 ARG A 49 TYR A 107 LYS A 112 PHE A 114
SITE 2 BC2 5 EDO A1400
SITE 1 BC3 6 ARG A 49 GLU A 118 ILE A 164 EDO A1399
SITE 2 BC3 6 HOH A2072 HOH A2146
SITE 1 BC4 5 PHE A 217 GLU A 218 VAL A 219 EDO A1393
SITE 2 BC4 5 HOH A2188
SITE 1 BC5 5 HIS A 332 ASP A 333 ASP A 358 ASN A 360
SITE 2 BC5 5 HOH A2292
SITE 1 BC6 6 ALA A 60 ALA A 133 TYR A 134 ARG A 258
SITE 2 BC6 6 ARG A 261 HOH A2321
SITE 1 BC7 4 SER A 85 ASP A 86 HIS A 89 HIS A 227
SITE 1 BC8 5 ARG A 171 HIS A 240 GLU A 243 HOH A2187
SITE 2 BC8 5 HOH A2229
SITE 1 BC9 3 GLY A 75 PRO A 116 GLU A 117
SITE 1 CC1 7 TYR A 149 GLY A 224 ASP A 225 THR A 226
SITE 2 CC1 7 HOH A2210 HOH A2211 HOH A2221
SITE 1 CC2 8 THR A 13 THR A 14 TYR A 15 GLY A 201
SITE 2 CC2 8 GLY A 202 EDO A1391 MG A1412 HOH A2294
SITE 1 CC3 8 ASP A 232 ASN A 235 ARG A 236 ASN A 239
SITE 2 CC3 8 LYS A 382 SER A 383 THR A 384 HOH A2226
SITE 1 CC4 5 ARG A 299 GLU A 303 LYS A 348 HOH A2269
SITE 2 CC4 5 HOH A2273
SITE 1 CC5 4 ARG A 262 GLU A 283 ILE A 284 ASP A 285
SITE 1 CC6 6 EDO A1391 EDO A1408 HOH A2006 HOH A2009
SITE 2 CC6 6 HOH A2189 HOH A2206
CRYST1 47.521 89.046 95.944 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 0.021043 0.000000 0.000000 0.00000
SCALE2 0.000000 0.011230 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010423 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
