HEADER CHAPERONE 15-MAR-13 4JNF
TITLE ALLOSTERIC OPENING OF THE POLYPEPTIDE-BINDING SITE WHEN AN HSP70 BINDS
TITLE 2 ATP
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HSP70 CHAPERONE DNAK;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: SUBSTRATE BINDING DOMAIN, UNP RESIDUES 389-610;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 83333;
SOURCE 4 STRAIN: K12;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PSMT
KEYWDS DNAK, CHAPERONE, 70KDA HEAT SHOCK PROTEIN (HSP70), SUBSTRATE BINDING
KEYWDS 2 DOMAIN (SBD)
EXPDTA X-RAY DIFFRACTION
AUTHOR R.QI,E.B.SARBENG,Q.LIU,K.Q.LE,X.XU,H.XU,J.YANG,J.L.WONG,C.VORVIS,
AUTHOR 2 W.A.HENDRICKSON,L.ZHOU,Q.LIU
REVDAT 5 20-SEP-23 4JNF 1 SEQADV
REVDAT 4 15-NOV-17 4JNF 1 REMARK
REVDAT 3 07-AUG-13 4JNF 1 JRNL
REVDAT 2 10-JUL-13 4JNF 1 JRNL
REVDAT 1 29-MAY-13 4JNF 0
JRNL AUTH R.QI,E.B.SARBENG,Q.LIU,K.Q.LE,X.XU,H.XU,J.YANG,J.L.WONG,
JRNL AUTH 2 C.VORVIS,W.A.HENDRICKSON,L.ZHOU,Q.LIU
JRNL TITL ALLOSTERIC OPENING OF THE POLYPEPTIDE-BINDING SITE WHEN AN
JRNL TITL 2 HSP70 BINDS ATP.
JRNL REF NAT.STRUCT.MOL.BIOL. V. 20 900 2013
JRNL REFN ISSN 1545-9993
JRNL PMID 23708608
JRNL DOI 10.1038/NSMB.2583
REMARK 2
REMARK 2 RESOLUTION. 1.62 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX
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 : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.62
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 29.71
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.2
REMARK 3 NUMBER OF REFLECTIONS : 42464
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.192
REMARK 3 R VALUE (WORKING SET) : 0.191
REMARK 3 FREE R VALUE : 0.216
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.640
REMARK 3 FREE R VALUE TEST SET COUNT : 1969
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 29.7155 - 3.9032 0.95 2982 150 0.2027 0.2384
REMARK 3 2 3.9032 - 3.0992 1.00 3013 144 0.1819 0.2071
REMARK 3 3 3.0992 - 2.7077 1.00 2964 143 0.1992 0.2203
REMARK 3 4 2.7077 - 2.4603 1.00 2951 138 0.1929 0.2265
REMARK 3 5 2.4603 - 2.2840 1.00 2963 144 0.1814 0.1909
REMARK 3 6 2.2840 - 2.1494 1.00 2925 139 0.1774 0.1916
REMARK 3 7 2.1494 - 2.0418 1.00 2895 137 0.1757 0.2110
REMARK 3 8 2.0418 - 1.9529 0.99 2914 148 0.1839 0.1886
REMARK 3 9 1.9529 - 1.8777 0.99 2894 141 0.1675 0.1764
REMARK 3 10 1.8777 - 1.8129 0.99 2832 139 0.1838 0.2132
REMARK 3 11 1.8129 - 1.7563 0.99 2880 142 0.1969 0.1966
REMARK 3 12 1.7563 - 1.7061 0.98 2853 136 0.2152 0.2700
REMARK 3 13 1.7061 - 1.6612 0.97 2813 139 0.2436 0.2651
REMARK 3 14 1.6612 - 1.6206 0.91 2616 129 0.2299 0.2562
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 : 0.38
REMARK 3 B_SOL : 46.00
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.190
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 18.340
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.00000
REMARK 3 B22 (A**2) : 0.00000
REMARK 3 B33 (A**2) : 0.00000
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 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 : 0.006 1621
REMARK 3 ANGLE : 0.844 2183
REMARK 3 CHIRALITY : 0.055 259
REMARK 3 PLANARITY : 0.003 289
REMARK 3 DIHEDRAL : 13.864 621
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 10
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: (CHAIN A AND RESID 388:421)
REMARK 3 ORIGIN FOR THE GROUP (A): 19.2011 22.8646 19.7264
REMARK 3 T TENSOR
REMARK 3 T11: 0.2035 T22: 0.1473
REMARK 3 T33: 0.1049 T12: 0.1158
REMARK 3 T13: 0.0318 T23: 0.0478
REMARK 3 L TENSOR
REMARK 3 L11: 0.0336 L22: 0.1993
REMARK 3 L33: 0.1718 L12: 0.0323
REMARK 3 L13: 0.0278 L23: -0.0203
REMARK 3 S TENSOR
REMARK 3 S11: -0.0688 S12: -0.0615 S13: -0.0343
REMARK 3 S21: 0.0655 S22: -0.0203 S23: -0.0421
REMARK 3 S31: 0.0673 S32: -0.0324 S33: -0.2448
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: (CHAIN A AND RESID 422:455)
REMARK 3 ORIGIN FOR THE GROUP (A): 10.9543 26.8268 11.8997
REMARK 3 T TENSOR
REMARK 3 T11: 0.1851 T22: 0.1564
REMARK 3 T33: 0.1279 T12: 0.0697
REMARK 3 T13: 0.0248 T23: 0.0056
REMARK 3 L TENSOR
REMARK 3 L11: 0.0585 L22: 0.4132
REMARK 3 L33: 0.9722 L12: -0.0128
REMARK 3 L13: -0.0487 L23: -0.2037
REMARK 3 S TENSOR
REMARK 3 S11: 0.0258 S12: 0.0446 S13: -0.0914
REMARK 3 S21: 0.0566 S22: 0.0052 S23: 0.1735
REMARK 3 S31: 0.0302 S32: -0.1792 S33: 0.2422
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: (CHAIN A AND RESID 456:464)
REMARK 3 ORIGIN FOR THE GROUP (A): -3.7348 25.6311 13.4005
REMARK 3 T TENSOR
REMARK 3 T11: 0.1859 T22: 0.3348
REMARK 3 T33: 0.4424 T12: 0.0140
REMARK 3 T13: -0.0412 T23: -0.0268
REMARK 3 L TENSOR
REMARK 3 L11: 0.0101 L22: 0.0039
REMARK 3 L33: 0.0087 L12: -0.0062
REMARK 3 L13: 0.0099 L23: -0.0060
REMARK 3 S TENSOR
REMARK 3 S11: -0.0560 S12: 0.0226 S13: 0.0916
REMARK 3 S21: -0.0814 S22: -0.0749 S23: 0.1583
REMARK 3 S31: -0.0123 S32: -0.3024 S33: 0.0000
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: (CHAIN A AND RESID 465:489)
REMARK 3 ORIGIN FOR THE GROUP (A): 5.0688 24.9931 22.0932
REMARK 3 T TENSOR
REMARK 3 T11: 0.2695 T22: 0.2071
REMARK 3 T33: 0.2317 T12: 0.0978
REMARK 3 T13: 0.0980 T23: 0.0549
REMARK 3 L TENSOR
REMARK 3 L11: 0.3370 L22: 0.2563
REMARK 3 L33: 0.1771 L12: 0.1677
REMARK 3 L13: 0.2235 L23: 0.1565
REMARK 3 S TENSOR
REMARK 3 S11: -0.0348 S12: -0.2593 S13: 0.1378
REMARK 3 S21: 0.3698 S22: 0.0546 S23: 0.2309
REMARK 3 S31: -0.1136 S32: -0.2543 S33: 0.0488
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: (CHAIN A AND RESID 490:496)
REMARK 3 ORIGIN FOR THE GROUP (A): -5.3060 27.6988 22.7046
REMARK 3 T TENSOR
REMARK 3 T11: 0.2457 T22: 0.4017
REMARK 3 T33: 0.6200 T12: 0.0801
REMARK 3 T13: 0.1529 T23: 0.0853
REMARK 3 L TENSOR
REMARK 3 L11: 0.0299 L22: 0.0997
REMARK 3 L33: 0.0654 L12: -0.0004
REMARK 3 L13: 0.0362 L23: 0.0240
REMARK 3 S TENSOR
REMARK 3 S11: 0.0230 S12: -0.0597 S13: 0.0755
REMARK 3 S21: 0.0014 S22: -0.0426 S23: 0.0126
REMARK 3 S31: -0.0181 S32: -0.0536 S33: -0.0464
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: (CHAIN A AND RESID 497:520)
REMARK 3 ORIGIN FOR THE GROUP (A): 20.1328 17.5509 10.8617
REMARK 3 T TENSOR
REMARK 3 T11: 0.2767 T22: 0.1943
REMARK 3 T33: 0.2342 T12: 0.2222
REMARK 3 T13: 0.0956 T23: 0.0329
REMARK 3 L TENSOR
REMARK 3 L11: 1.3089 L22: 0.3025
REMARK 3 L33: 0.7202 L12: -0.5614
REMARK 3 L13: -0.1493 L23: 0.2548
REMARK 3 S TENSOR
REMARK 3 S11: -0.1348 S12: -0.0688 S13: -0.5188
REMARK 3 S21: 0.0358 S22: -0.0405 S23: 0.2357
REMARK 3 S31: 0.5595 S32: 0.1315 S33: 0.2326
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: (CHAIN A AND RESID 521:549)
REMARK 3 ORIGIN FOR THE GROUP (A): 10.5887 42.4766 7.7344
REMARK 3 T TENSOR
REMARK 3 T11: 0.1978 T22: 0.1327
REMARK 3 T33: 0.1202 T12: 0.0826
REMARK 3 T13: 0.0544 T23: 0.0177
REMARK 3 L TENSOR
REMARK 3 L11: 0.7029 L22: 0.7929
REMARK 3 L33: 0.5448 L12: 0.3149
REMARK 3 L13: -0.0702 L23: 0.0861
REMARK 3 S TENSOR
REMARK 3 S11: 0.0487 S12: -0.0656 S13: 0.1771
REMARK 3 S21: 0.0748 S22: 0.0361 S23: 0.2181
REMARK 3 S31: -0.1223 S32: 0.0488 S33: -0.0028
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: (CHAIN A AND RESID 550:558)
REMARK 3 ORIGIN FOR THE GROUP (A): -12.2180 56.5995 10.5129
REMARK 3 T TENSOR
REMARK 3 T11: 0.3559 T22: 0.3517
REMARK 3 T33: 0.6005 T12: 0.2218
REMARK 3 T13: 0.1246 T23: 0.0339
REMARK 3 L TENSOR
REMARK 3 L11: 0.1363 L22: 0.0736
REMARK 3 L33: 0.2368 L12: -0.0953
REMARK 3 L13: -0.0564 L23: 0.0017
REMARK 3 S TENSOR
REMARK 3 S11: 0.0054 S12: -0.0173 S13: -0.0297
REMARK 3 S21: -0.0032 S22: -0.0190 S23: 0.0362
REMARK 3 S31: 0.0131 S32: -0.0270 S33: 0.0234
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: (CHAIN A AND RESID 559:579)
REMARK 3 ORIGIN FOR THE GROUP (A): 1.4034 54.8814 2.1733
REMARK 3 T TENSOR
REMARK 3 T11: 0.2976 T22: 0.1584
REMARK 3 T33: 0.2335 T12: 0.2822
REMARK 3 T13: 0.0796 T23: 0.0358
REMARK 3 L TENSOR
REMARK 3 L11: 0.0785 L22: 0.5551
REMARK 3 L33: 0.1319 L12: 0.0986
REMARK 3 L13: 0.0264 L23: 0.0612
REMARK 3 S TENSOR
REMARK 3 S11: 0.0242 S12: 0.0652 S13: 0.0991
REMARK 3 S21: -0.0129 S22: 0.0197 S23: 0.3991
REMARK 3 S31: -0.2907 S32: -0.2406 S33: 0.1189
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: (CHAIN A AND RESID 580:604)
REMARK 3 ORIGIN FOR THE GROUP (A): 3.2817 56.1784 11.8714
REMARK 3 T TENSOR
REMARK 3 T11: 0.3415 T22: 0.1856
REMARK 3 T33: 0.2250 T12: 0.1910
REMARK 3 T13: 0.1479 T23: 0.0603
REMARK 3 L TENSOR
REMARK 3 L11: 0.2476 L22: 0.0282
REMARK 3 L33: 0.0312 L12: 0.0816
REMARK 3 L13: 0.0867 L23: 0.0291
REMARK 3 S TENSOR
REMARK 3 S11: -0.0078 S12: -0.3014 S13: 0.0628
REMARK 3 S21: 0.3455 S22: 0.1566 S23: 0.3925
REMARK 3 S31: -0.3608 S32: -0.2700 S33: 0.0767
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 4JNF COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 18-MAR-13.
REMARK 100 THE DEPOSITION ID IS D_1000078265.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 17-AUG-11
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : NSLS
REMARK 200 BEAMLINE : X4C
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97915
REMARK 200 MONOCHROMATOR : SI 111 CHANNEL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MAR CCD 165 MM
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 42873
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.620
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.9
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.62
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.65
REMARK 200 COMPLETENESS FOR SHELL (%) : 86.8
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> 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: MOLREP
REMARK 200 STARTING MODEL: PDB ENTRY 1DKX
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 64.59
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.47
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 2.0 M AMMONIUM SULFATE, 0.1 M TRIS
REMARK 280 -HCL, PH 8.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+1/3
REMARK 290 3555 -X+Y,-X,Z+2/3
REMARK 290 4555 Y,X,-Z
REMARK 290 5555 X-Y,-Y,-Z+2/3
REMARK 290 6555 -X,-X+Y,-Z+1/3
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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 42.91967
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 85.83933
REMARK 290 SMTRY1 4 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 4 0.866025 0.500000 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 85.83933
REMARK 290 SMTRY1 6 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 42.91967
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 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH A 984 LIES ON A SPECIAL POSITION.
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 GLN A 605
REMARK 465 HIS A 606
REMARK 465 ALA A 607
REMARK 465 GLN A 608
REMARK 465 GLN A 609
REMARK 465 GLN A 610
REMARK 465 HIS A 611
REMARK 465 ALA A 612
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 495 CG CD CE NZ
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 ARG A 467 15.78 59.91
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1DKZ RELATED DB: PDB
REMARK 900 SUBSTRATE BINDING DOMAIN OF DNAK WITH A SUBSTRATE PEPTIDE
REMARK 900 RELATED ID: 4JN4 RELATED DB: PDB
REMARK 900 RELATED ID: 4JNE RELATED DB: PDB
DBREF 4JNF A 389 610 UNP P0A6Y8 DNAK_ECOLI 389 610
SEQADV 4JNF SER A 388 UNP P0A6Y8 EXPRESSION TAG
SEQADV 4JNF A UNP P0A6Y8 THR 428 DELETION
SEQADV 4JNF A UNP P0A6Y8 ALA 429 DELETION
SEQADV 4JNF A UNP P0A6Y8 GLU 430 DELETION
SEQADV 4JNF A UNP P0A6Y8 ASP 431 DELETION
SEQADV 4JNF MET A 428 UNP P0A6Y8 ASN 432 ENGINEERED MUTATION
SEQADV 4JNF GLY A 429 UNP P0A6Y8 GLN 433 ENGINEERED MUTATION
SEQADV 4JNF GLY A 430 UNP P0A6Y8 SER 434 ENGINEERED MUTATION
SEQADV 4JNF HIS A 611 UNP P0A6Y8 EXPRESSION TAG
SEQADV 4JNF ALA A 612 UNP P0A6Y8 EXPRESSION TAG
SEQRES 1 A 221 SER VAL LEU LEU LEU ASP VAL THR PRO LEU SER LEU GLY
SEQRES 2 A 221 ILE GLU THR MET GLY GLY VAL MET THR THR LEU ILE ALA
SEQRES 3 A 221 LYS ASN THR THR ILE PRO THR LYS HIS SER GLN VAL PHE
SEQRES 4 A 221 SER MET GLY GLY ALA VAL THR ILE HIS VAL LEU GLN GLY
SEQRES 5 A 221 GLU ARG LYS ARG ALA ALA ASP ASN LYS SER LEU GLY GLN
SEQRES 6 A 221 PHE ASN LEU ASP GLY ILE ASN PRO ALA PRO ARG GLY MET
SEQRES 7 A 221 PRO GLN ILE GLU VAL THR PHE ASP ILE ASP ALA ASP GLY
SEQRES 8 A 221 ILE LEU HIS VAL SER ALA LYS ASP LYS ASN SER GLY LYS
SEQRES 9 A 221 GLU GLN LYS ILE THR ILE LYS ALA SER SER GLY LEU ASN
SEQRES 10 A 221 GLU ASP GLU ILE GLN LYS MET VAL ARG ASP ALA GLU ALA
SEQRES 11 A 221 ASN ALA GLU ALA ASP ARG LYS PHE GLU GLU LEU VAL GLN
SEQRES 12 A 221 THR ARG ASN GLN GLY ASP HIS LEU LEU HIS SER THR ARG
SEQRES 13 A 221 LYS GLN VAL GLU GLU ALA GLY ASP LYS LEU PRO ALA ASP
SEQRES 14 A 221 ASP LYS THR ALA ILE GLU SER ALA LEU THR ALA LEU GLU
SEQRES 15 A 221 THR ALA LEU LYS GLY GLU ASP LYS ALA ALA ILE GLU ALA
SEQRES 16 A 221 LYS MET GLN GLU LEU ALA GLN VAL SER GLN LYS LEU MET
SEQRES 17 A 221 GLU ILE ALA GLN GLN GLN HIS ALA GLN GLN GLN HIS ALA
FORMUL 2 HOH *321(H2 O)
HELIX 1 1 ARG A 447 ASN A 451 5 5
HELIX 2 2 ALA A 465 MET A 469 5 5
HELIX 3 3 LYS A 502 GLY A 506 5 5
HELIX 4 4 ASN A 508 ASN A 522 1 15
HELIX 5 5 ASN A 522 GLY A 554 1 33
HELIX 6 6 ASP A 555 LEU A 557 5 3
HELIX 7 7 PRO A 558 LYS A 577 1 20
HELIX 8 8 ASP A 580 VAL A 594 1 15
HELIX 9 9 SER A 595 GLN A 604 1 10
SHEET 1 A 4 VAL A 407 ILE A 412 0
SHEET 2 A 4 LEU A 399 THR A 403 -1 N LEU A 399 O LEU A 411
SHEET 3 A 4 VAL A 436 GLN A 442 -1 O LEU A 441 N GLY A 400
SHEET 4 A 4 LYS A 452 LEU A 459 -1 O PHE A 457 N ILE A 438
SHEET 1 B 4 THR A 420 PHE A 426 0
SHEET 2 B 4 ILE A 472 ILE A 478 -1 O PHE A 476 N HIS A 422
SHEET 3 B 4 LEU A 484 ASP A 490 -1 O HIS A 485 N ASP A 477
SHEET 4 B 4 GLU A 496 THR A 500 -1 O ILE A 499 N VAL A 486
CISPEP 1 ILE A 418 PRO A 419 0 0.61
CRYST1 66.980 66.980 128.759 90.00 90.00 120.00 P 31 2 1 6
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 0.014930 0.008620 0.000000 0.00000
SCALE2 0.000000 0.017239 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007766 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
