HEADER SIGNALING PROTEIN 07-SEP-16 5LU1
TITLE HUMAN 14-3-3 SIGMA CLU3 MUTANT COMPLEXED WITH SHORT HSPB6
TITLE 2 PHOSPHOPEPTIDE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: 14-3-3 PROTEIN SIGMA;
COMPND 3 CHAIN: A, B, E, F;
COMPND 4 FRAGMENT: UNP RESIDUES 1-231;
COMPND 5 SYNONYM: EPITHELIAL CELL MARKER PROTEIN 1,STRATIFIN;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES;
COMPND 8 MOL_ID: 2;
COMPND 9 MOLECULE: HEAT SHOCK PROTEIN BETA-6;
COMPND 10 CHAIN: C, D, G, H;
COMPND 11 FRAGMENT: UNP RESIDUES 13-20;
COMPND 12 SYNONYM: HSPB6,HEAT SHOCK 20 KDA-LIKE PROTEIN P20;
COMPND 13 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: SFN, HME1;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 MOL_ID: 2;
SOURCE 9 SYNTHETIC: YES;
SOURCE 10 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 11 ORGANISM_COMMON: HUMAN;
SOURCE 12 ORGANISM_TAXID: 9606
KEYWDS PROTEIN-PEPTIDE COMPLEX, INTRINSICALLY DISORDERED PROTEIN REGION(S),
KEYWDS 2 SIGNALING PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR N.N.SLUCHANKO,S.BEELEN,A.A.KULIKOVA,S.D.WEEKS,A.A.ANTSON,N.B.GUSEV,
AUTHOR 2 S.V.STRELKOV
REVDAT 3 17-JAN-24 5LU1 1 REMARK
REVDAT 2 15-FEB-17 5LU1 1 JRNL
REVDAT 1 01-FEB-17 5LU1 0
JRNL AUTH N.N.SLUCHANKO,S.BEELEN,A.A.KULIKOVA,S.D.WEEKS,A.A.ANTSON,
JRNL AUTH 2 N.B.GUSEV,S.V.STRELKOV
JRNL TITL STRUCTURAL BASIS FOR THE INTERACTION OF A HUMAN SMALL HEAT
JRNL TITL 2 SHOCK PROTEIN WITH THE 14-3-3 UNIVERSAL SIGNALING REGULATOR.
JRNL REF STRUCTURE V. 25 305 2017
JRNL REFN ISSN 1878-4186
JRNL PMID 28089448
JRNL DOI 10.1016/J.STR.2016.12.005
REMARK 2
REMARK 2 RESOLUTION. 2.40 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : BUSTER-TNT 2.10.3
REMARK 3 AUTHORS : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER,
REMARK 3 : PACIOREK,ROVERSI,SMART,VONRHEIN,WOMACK,
REMARK 3 : MATTHEWS,TEN EYCK,TRONRUD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.40
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 47.89
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 3 NUMBER OF REFLECTIONS : 54511
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) : 0.186
REMARK 3 R VALUE (WORKING SET) : 0.184
REMARK 3 FREE R VALUE : 0.214
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.990
REMARK 3 FREE R VALUE TEST SET COUNT : 2718
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.000
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) : 2.40
REMARK 3 BIN RESOLUTION RANGE LOW (ANGSTROMS) : 2.46
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.97
REMARK 3 REFLECTIONS IN BIN (WORKING + TEST SET) : 4009
REMARK 3 BIN R VALUE (WORKING + TEST SET) : NULL
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 3808
REMARK 3 BIN R VALUE (WORKING SET) : 0.2290
REMARK 3 BIN FREE R VALUE : 0.2760
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5.01
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 201
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 : 7449
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 32
REMARK 3 SOLVENT ATOMS : 361
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 66.17
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 72.11
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 1.00670
REMARK 3 B22 (A**2) : 6.01250
REMARK 3 B33 (A**2) : -7.01930
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 6.64280
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.310
REMARK 3 DPI (BLOW EQ-10) BASED ON R VALUE (A) : 0.255
REMARK 3 DPI (BLOW EQ-9) BASED ON FREE R VALUE (A) : 0.192
REMARK 3 DPI (CRUICKSHANK) BASED ON R VALUE (A) : 0.257
REMARK 3 DPI (CRUICKSHANK) BASED ON FREE R VALUE (A) : 0.195
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 : 0.949
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.938
REMARK 3
REMARK 3 NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15
REMARK 3 TERM COUNT WEIGHT FUNCTION.
REMARK 3 BOND LENGTHS : 7587 ; 2.000 ; HARMONIC
REMARK 3 BOND ANGLES : 10217 ; 2.000 ; HARMONIC
REMARK 3 TORSION ANGLES : 2761 ; 2.000 ; SINUSOIDAL
REMARK 3 TRIGONAL CARBON PLANES : 219 ; 2.000 ; HARMONIC
REMARK 3 GENERAL PLANES : 1072 ; 5.000 ; HARMONIC
REMARK 3 ISOTROPIC THERMAL FACTORS : 7587 ; 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 : 975 ; 5.000 ; SEMIHARMONIC
REMARK 3 SUM OF OCCUPANCIES : NULL ; NULL ; NULL
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 : 9093 ; 4.000 ; SEMIHARMONIC
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.010
REMARK 3 BOND ANGLES (DEGREES) : 1.64
REMARK 3 PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 2.90
REMARK 3 OTHER TORSION ANGLES (DEGREES) : 18.81
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 4
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: { A|* C|* }
REMARK 3 ORIGIN FOR THE GROUP (A): 18.0120 -18.6210 14.7127
REMARK 3 T TENSOR
REMARK 3 T11: 0.0305 T22: -0.0467
REMARK 3 T33: -0.0069 T12: 0.0517
REMARK 3 T13: -0.0701 T23: 0.0285
REMARK 3 L TENSOR
REMARK 3 L11: 1.0539 L22: 3.2839
REMARK 3 L33: 1.3875 L12: 0.6027
REMARK 3 L13: 0.5000 L23: 1.0066
REMARK 3 S TENSOR
REMARK 3 S11: 0.1662 S12: 0.1033 S13: -0.2461
REMARK 3 S21: 0.2024 S22: 0.0625 S23: -0.1678
REMARK 3 S31: 0.3232 S32: 0.0411 S33: -0.2287
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: { B|* D|* }
REMARK 3 ORIGIN FOR THE GROUP (A): 11.7520 19.1170 18.7670
REMARK 3 T TENSOR
REMARK 3 T11: -0.1151 T22: -0.0520
REMARK 3 T33: -0.0405 T12: -0.0293
REMARK 3 T13: -0.0003 T23: -0.0414
REMARK 3 L TENSOR
REMARK 3 L11: 1.9633 L22: 2.6202
REMARK 3 L33: 1.3173 L12: -0.6915
REMARK 3 L13: 0.4639 L23: -0.2718
REMARK 3 S TENSOR
REMARK 3 S11: -0.1696 S12: -0.0630 S13: 0.2065
REMARK 3 S21: 0.1792 S22: 0.0073 S23: 0.0939
REMARK 3 S31: -0.1197 S32: -0.0021 S33: 0.1623
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: { E|* G|* }
REMARK 3 ORIGIN FOR THE GROUP (A): 41.8880 -27.3700 49.0290
REMARK 3 T TENSOR
REMARK 3 T11: 0.0310 T22: 0.1292
REMARK 3 T33: -0.0152 T12: -0.0972
REMARK 3 T13: 0.0595 T23: -0.1011
REMARK 3 L TENSOR
REMARK 3 L11: 2.3310 L22: 2.7778
REMARK 3 L33: 2.6221 L12: -0.3469
REMARK 3 L13: 0.5335 L23: 1.1123
REMARK 3 S TENSOR
REMARK 3 S11: 0.0528 S12: -0.4294 S13: 0.3782
REMARK 3 S21: 0.0677 S22: 0.1391 S23: -0.2671
REMARK 3 S31: -0.3924 S32: 0.2297 S33: -0.1920
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: { F|* H|* }
REMARK 3 ORIGIN FOR THE GROUP (A): 33.3580 -63.2380 38.9990
REMARK 3 T TENSOR
REMARK 3 T11: -0.0894 T22: 0.0204
REMARK 3 T33: -0.0246 T12: 0.0267
REMARK 3 T13: 0.0080 T23: 0.0277
REMARK 3 L TENSOR
REMARK 3 L11: 1.9518 L22: 2.4024
REMARK 3 L33: 1.7841 L12: 0.8462
REMARK 3 L13: 0.3205 L23: 0.2132
REMARK 3 S TENSOR
REMARK 3 S11: -0.0554 S12: -0.2493 S13: -0.3008
REMARK 3 S21: 0.0006 S22: 0.1098 S23: 0.0324
REMARK 3 S31: 0.1495 S32: -0.0319 S33: -0.0544
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 5LU1 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 07-SEP-16.
REMARK 100 THE DEPOSITION ID IS D_1200001357.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 12-JUN-15
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 : SOLEIL
REMARK 200 BEAMLINE : PROXIMA 2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9801
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 : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 54513
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.400
REMARK 200 RESOLUTION RANGE LOW (A) : 48.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 200 DATA REDUNDANCY : 3.700
REMARK 200 R MERGE (I) : 0.09900
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 8.6100
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.40
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.46
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.9
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 1.53300
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 0.900
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: 3IQJ
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 62.30
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.26
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M BIS-TRIS PROPANE (PH 6.5), 0.2 M
REMARK 280 NANO3 AND 20% PEG 3350, VAPOR DIFFUSION, SITTING DROP,
REMARK 280 TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,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 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 52.00500
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 4840 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 22080 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -21.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D
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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 4960 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 22260 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -22.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, F, G, H
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 -2
REMARK 465 PRO A -1
REMARK 465 HIS A 0
REMARK 465 MET A 1
REMARK 465 GLU A 72
REMARK 465 GLY A 73
REMARK 465 SER A 74
REMARK 465 ALA A 75
REMARK 465 ALA A 76
REMARK 465 GLU B 71
REMARK 465 GLU B 72
REMARK 465 GLY B 73
REMARK 465 SER B 74
REMARK 465 ALA B 75
REMARK 465 ALA B 76
REMARK 465 ALA B 77
REMARK 465 GLY E -2
REMARK 465 GLU E 72
REMARK 465 GLY E 73
REMARK 465 SER E 74
REMARK 465 ALA E 75
REMARK 465 ALA E 76
REMARK 465 ALA E 77
REMARK 465 GLU F 72
REMARK 465 GLY F 73
REMARK 465 SER F 74
REMARK 465 ALA F 75
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 OD2 ASP F 139 O3 TRS F 501 1.83
REMARK 500 OD2 ASP A 139 O3 TRS A 501 1.89
REMARK 500 OD2 ASP E 97 O1 TRS E 501 1.96
REMARK 500 OD2 ASP B 97 O1 TRS B 501 1.97
REMARK 500 OD2 ASP E 139 O3 TRS E 501 2.01
REMARK 500 OD2 ASP F 97 O1 TRS F 501 2.04
REMARK 500 OD2 ASP A 97 O1 TRS A 501 2.06
REMARK 500 OD2 ASP B 139 O3 TRS B 501 2.07
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 ARG A 18 76.49 -105.27
REMARK 500 HIS A 106 -40.87 -133.20
REMARK 500 THR A 136 -57.06 -124.15
REMARK 500 ARG B 18 77.55 -107.27
REMARK 500 HIS B 106 -37.36 -132.08
REMARK 500 THR B 136 -56.79 -124.53
REMARK 500 ARG E 18 76.33 -107.05
REMARK 500 HIS E 106 -41.15 -134.85
REMARK 500 THR E 136 -56.97 -124.53
REMARK 500 ARG F 18 76.99 -107.08
REMARK 500 HIS F 106 -41.99 -135.24
REMARK 500 THR F 136 -54.30 -124.74
REMARK 500 LEU F 208 147.74 -28.16
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 A 692 DISTANCE = 8.67 ANGSTROMS
REMARK 525 HOH A 693 DISTANCE = 8.79 ANGSTROMS
REMARK 525 HOH B 692 DISTANCE = 14.90 ANGSTROMS
REMARK 525 HOH D 114 DISTANCE = 6.06 ANGSTROMS
REMARK 525 HOH E 666 DISTANCE = 9.46 ANGSTROMS
REMARK 525 HOH E 667 DISTANCE = 12.09 ANGSTROMS
REMARK 525 HOH F 678 DISTANCE = 9.56 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue TRS A 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue TRS B 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue TRS E 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue TRS F 501
DBREF 5LU1 A 1 231 UNP P31947 1433S_HUMAN 1 231
DBREF 5LU1 B 1 231 UNP P31947 1433S_HUMAN 1 231
DBREF 5LU1 C 13 20 UNP O14558 HSPB6_HUMAN 13 20
DBREF 5LU1 D 13 20 UNP O14558 HSPB6_HUMAN 13 20
DBREF 5LU1 E 1 231 UNP P31947 1433S_HUMAN 1 231
DBREF 5LU1 F 1 231 UNP P31947 1433S_HUMAN 1 231
DBREF 5LU1 G 13 20 UNP O14558 HSPB6_HUMAN 13 20
DBREF 5LU1 H 13 20 UNP O14558 HSPB6_HUMAN 13 20
SEQADV 5LU1 GLY A -2 UNP P31947 EXPRESSION TAG
SEQADV 5LU1 PRO A -1 UNP P31947 EXPRESSION TAG
SEQADV 5LU1 HIS A 0 UNP P31947 EXPRESSION TAG
SEQADV 5LU1 ALA A 75 UNP P31947 GLU 75 ENGINEERED MUTATION
SEQADV 5LU1 ALA A 76 UNP P31947 GLU 76 ENGINEERED MUTATION
SEQADV 5LU1 ALA A 77 UNP P31947 LYS 77 ENGINEERED MUTATION
SEQADV 5LU1 GLY B -2 UNP P31947 EXPRESSION TAG
SEQADV 5LU1 PRO B -1 UNP P31947 EXPRESSION TAG
SEQADV 5LU1 HIS B 0 UNP P31947 EXPRESSION TAG
SEQADV 5LU1 ALA B 75 UNP P31947 GLU 75 ENGINEERED MUTATION
SEQADV 5LU1 ALA B 76 UNP P31947 GLU 76 ENGINEERED MUTATION
SEQADV 5LU1 ALA B 77 UNP P31947 LYS 77 ENGINEERED MUTATION
SEQADV 5LU1 GLY E -2 UNP P31947 EXPRESSION TAG
SEQADV 5LU1 PRO E -1 UNP P31947 EXPRESSION TAG
SEQADV 5LU1 HIS E 0 UNP P31947 EXPRESSION TAG
SEQADV 5LU1 ALA E 75 UNP P31947 GLU 75 ENGINEERED MUTATION
SEQADV 5LU1 ALA E 76 UNP P31947 GLU 76 ENGINEERED MUTATION
SEQADV 5LU1 ALA E 77 UNP P31947 LYS 77 ENGINEERED MUTATION
SEQADV 5LU1 GLY F -2 UNP P31947 EXPRESSION TAG
SEQADV 5LU1 PRO F -1 UNP P31947 EXPRESSION TAG
SEQADV 5LU1 HIS F 0 UNP P31947 EXPRESSION TAG
SEQADV 5LU1 ALA F 75 UNP P31947 GLU 75 ENGINEERED MUTATION
SEQADV 5LU1 ALA F 76 UNP P31947 GLU 76 ENGINEERED MUTATION
SEQADV 5LU1 ALA F 77 UNP P31947 LYS 77 ENGINEERED MUTATION
SEQRES 1 A 234 GLY PRO HIS MET GLU ARG ALA SER LEU ILE GLN LYS ALA
SEQRES 2 A 234 LYS LEU ALA GLU GLN ALA GLU ARG TYR GLU ASP MET ALA
SEQRES 3 A 234 ALA PHE MET LYS GLY ALA VAL GLU LYS GLY GLU GLU LEU
SEQRES 4 A 234 SER CYS GLU GLU ARG ASN LEU LEU SER VAL ALA TYR LYS
SEQRES 5 A 234 ASN VAL VAL GLY GLY GLN ARG ALA ALA TRP ARG VAL LEU
SEQRES 6 A 234 SER SER ILE GLU GLN LYS SER ASN GLU GLU GLY SER ALA
SEQRES 7 A 234 ALA ALA GLY PRO GLU VAL ARG GLU TYR ARG GLU LYS VAL
SEQRES 8 A 234 GLU THR GLU LEU GLN GLY VAL CYS ASP THR VAL LEU GLY
SEQRES 9 A 234 LEU LEU ASP SER HIS LEU ILE LYS GLU ALA GLY ASP ALA
SEQRES 10 A 234 GLU SER ARG VAL PHE TYR LEU LYS MET LYS GLY ASP TYR
SEQRES 11 A 234 TYR ARG TYR LEU ALA GLU VAL ALA THR GLY ASP ASP LYS
SEQRES 12 A 234 LYS ARG ILE ILE ASP SER ALA ARG SER ALA TYR GLN GLU
SEQRES 13 A 234 ALA MET ASP ILE SER LYS LYS GLU MET PRO PRO THR ASN
SEQRES 14 A 234 PRO ILE ARG LEU GLY LEU ALA LEU ASN PHE SER VAL PHE
SEQRES 15 A 234 HIS TYR GLU ILE ALA ASN SER PRO GLU GLU ALA ILE SER
SEQRES 16 A 234 LEU ALA LYS THR THR PHE ASP GLU ALA MET ALA ASP LEU
SEQRES 17 A 234 HIS THR LEU SER GLU ASP SER TYR LYS ASP SER THR LEU
SEQRES 18 A 234 ILE MET GLN LEU LEU ARG ASP ASN LEU THR LEU TRP THR
SEQRES 1 B 234 GLY PRO HIS MET GLU ARG ALA SER LEU ILE GLN LYS ALA
SEQRES 2 B 234 LYS LEU ALA GLU GLN ALA GLU ARG TYR GLU ASP MET ALA
SEQRES 3 B 234 ALA PHE MET LYS GLY ALA VAL GLU LYS GLY GLU GLU LEU
SEQRES 4 B 234 SER CYS GLU GLU ARG ASN LEU LEU SER VAL ALA TYR LYS
SEQRES 5 B 234 ASN VAL VAL GLY GLY GLN ARG ALA ALA TRP ARG VAL LEU
SEQRES 6 B 234 SER SER ILE GLU GLN LYS SER ASN GLU GLU GLY SER ALA
SEQRES 7 B 234 ALA ALA GLY PRO GLU VAL ARG GLU TYR ARG GLU LYS VAL
SEQRES 8 B 234 GLU THR GLU LEU GLN GLY VAL CYS ASP THR VAL LEU GLY
SEQRES 9 B 234 LEU LEU ASP SER HIS LEU ILE LYS GLU ALA GLY ASP ALA
SEQRES 10 B 234 GLU SER ARG VAL PHE TYR LEU LYS MET LYS GLY ASP TYR
SEQRES 11 B 234 TYR ARG TYR LEU ALA GLU VAL ALA THR GLY ASP ASP LYS
SEQRES 12 B 234 LYS ARG ILE ILE ASP SER ALA ARG SER ALA TYR GLN GLU
SEQRES 13 B 234 ALA MET ASP ILE SER LYS LYS GLU MET PRO PRO THR ASN
SEQRES 14 B 234 PRO ILE ARG LEU GLY LEU ALA LEU ASN PHE SER VAL PHE
SEQRES 15 B 234 HIS TYR GLU ILE ALA ASN SER PRO GLU GLU ALA ILE SER
SEQRES 16 B 234 LEU ALA LYS THR THR PHE ASP GLU ALA MET ALA ASP LEU
SEQRES 17 B 234 HIS THR LEU SER GLU ASP SER TYR LYS ASP SER THR LEU
SEQRES 18 B 234 ILE MET GLN LEU LEU ARG ASP ASN LEU THR LEU TRP THR
SEQRES 1 C 8 ARG ARG ALA SEP ALA PRO LEU PRO
SEQRES 1 D 8 ARG ARG ALA SEP ALA PRO LEU PRO
SEQRES 1 E 234 GLY PRO HIS MET GLU ARG ALA SER LEU ILE GLN LYS ALA
SEQRES 2 E 234 LYS LEU ALA GLU GLN ALA GLU ARG TYR GLU ASP MET ALA
SEQRES 3 E 234 ALA PHE MET LYS GLY ALA VAL GLU LYS GLY GLU GLU LEU
SEQRES 4 E 234 SER CYS GLU GLU ARG ASN LEU LEU SER VAL ALA TYR LYS
SEQRES 5 E 234 ASN VAL VAL GLY GLY GLN ARG ALA ALA TRP ARG VAL LEU
SEQRES 6 E 234 SER SER ILE GLU GLN LYS SER ASN GLU GLU GLY SER ALA
SEQRES 7 E 234 ALA ALA GLY PRO GLU VAL ARG GLU TYR ARG GLU LYS VAL
SEQRES 8 E 234 GLU THR GLU LEU GLN GLY VAL CYS ASP THR VAL LEU GLY
SEQRES 9 E 234 LEU LEU ASP SER HIS LEU ILE LYS GLU ALA GLY ASP ALA
SEQRES 10 E 234 GLU SER ARG VAL PHE TYR LEU LYS MET LYS GLY ASP TYR
SEQRES 11 E 234 TYR ARG TYR LEU ALA GLU VAL ALA THR GLY ASP ASP LYS
SEQRES 12 E 234 LYS ARG ILE ILE ASP SER ALA ARG SER ALA TYR GLN GLU
SEQRES 13 E 234 ALA MET ASP ILE SER LYS LYS GLU MET PRO PRO THR ASN
SEQRES 14 E 234 PRO ILE ARG LEU GLY LEU ALA LEU ASN PHE SER VAL PHE
SEQRES 15 E 234 HIS TYR GLU ILE ALA ASN SER PRO GLU GLU ALA ILE SER
SEQRES 16 E 234 LEU ALA LYS THR THR PHE ASP GLU ALA MET ALA ASP LEU
SEQRES 17 E 234 HIS THR LEU SER GLU ASP SER TYR LYS ASP SER THR LEU
SEQRES 18 E 234 ILE MET GLN LEU LEU ARG ASP ASN LEU THR LEU TRP THR
SEQRES 1 F 234 GLY PRO HIS MET GLU ARG ALA SER LEU ILE GLN LYS ALA
SEQRES 2 F 234 LYS LEU ALA GLU GLN ALA GLU ARG TYR GLU ASP MET ALA
SEQRES 3 F 234 ALA PHE MET LYS GLY ALA VAL GLU LYS GLY GLU GLU LEU
SEQRES 4 F 234 SER CYS GLU GLU ARG ASN LEU LEU SER VAL ALA TYR LYS
SEQRES 5 F 234 ASN VAL VAL GLY GLY GLN ARG ALA ALA TRP ARG VAL LEU
SEQRES 6 F 234 SER SER ILE GLU GLN LYS SER ASN GLU GLU GLY SER ALA
SEQRES 7 F 234 ALA ALA GLY PRO GLU VAL ARG GLU TYR ARG GLU LYS VAL
SEQRES 8 F 234 GLU THR GLU LEU GLN GLY VAL CYS ASP THR VAL LEU GLY
SEQRES 9 F 234 LEU LEU ASP SER HIS LEU ILE LYS GLU ALA GLY ASP ALA
SEQRES 10 F 234 GLU SER ARG VAL PHE TYR LEU LYS MET LYS GLY ASP TYR
SEQRES 11 F 234 TYR ARG TYR LEU ALA GLU VAL ALA THR GLY ASP ASP LYS
SEQRES 12 F 234 LYS ARG ILE ILE ASP SER ALA ARG SER ALA TYR GLN GLU
SEQRES 13 F 234 ALA MET ASP ILE SER LYS LYS GLU MET PRO PRO THR ASN
SEQRES 14 F 234 PRO ILE ARG LEU GLY LEU ALA LEU ASN PHE SER VAL PHE
SEQRES 15 F 234 HIS TYR GLU ILE ALA ASN SER PRO GLU GLU ALA ILE SER
SEQRES 16 F 234 LEU ALA LYS THR THR PHE ASP GLU ALA MET ALA ASP LEU
SEQRES 17 F 234 HIS THR LEU SER GLU ASP SER TYR LYS ASP SER THR LEU
SEQRES 18 F 234 ILE MET GLN LEU LEU ARG ASP ASN LEU THR LEU TRP THR
SEQRES 1 G 8 ARG ARG ALA SEP ALA PRO LEU PRO
SEQRES 1 H 8 ARG ARG ALA SEP ALA PRO LEU PRO
MODRES 5LU1 SEP C 16 SER MODIFIED RESIDUE
MODRES 5LU1 SEP D 16 SER MODIFIED RESIDUE
MODRES 5LU1 SEP G 16 SER MODIFIED RESIDUE
MODRES 5LU1 SEP H 16 SER MODIFIED RESIDUE
HET SEP C 16 10
HET SEP D 16 10
HET SEP G 16 10
HET SEP H 16 10
HET TRS A 501 8
HET TRS B 501 8
HET TRS E 501 8
HET TRS F 501 8
HETNAM SEP PHOSPHOSERINE
HETNAM TRS 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL
HETSYN SEP PHOSPHONOSERINE
HETSYN TRS TRIS BUFFER
FORMUL 3 SEP 4(C3 H8 N O6 P)
FORMUL 9 TRS 4(C4 H12 N O3 1+)
FORMUL 13 HOH *361(H2 O)
HELIX 1 AA1 GLU A 2 ALA A 16 1 15
HELIX 2 AA2 ARG A 18 GLU A 31 1 14
HELIX 3 AA3 SER A 37 SER A 69 1 33
HELIX 4 AA4 GLY A 78 HIS A 106 1 29
HELIX 5 AA5 HIS A 106 ALA A 111 1 6
HELIX 6 AA6 ASP A 113 ALA A 135 1 23
HELIX 7 AA7 GLY A 137 MET A 162 1 26
HELIX 8 AA8 ASN A 166 ILE A 183 1 18
HELIX 9 AA9 SER A 186 ASP A 204 1 19
HELIX 10 AB1 LEU A 205 LEU A 208 5 4
HELIX 11 AB2 SER A 209 ASP A 211 5 3
HELIX 12 AB3 SER A 212 THR A 231 1 20
HELIX 13 AB4 PRO B -1 ALA B 16 1 18
HELIX 14 AB5 ARG B 18 GLU B 31 1 14
HELIX 15 AB6 SER B 37 SER B 69 1 33
HELIX 16 AB7 PRO B 79 HIS B 106 1 28
HELIX 17 AB8 ASP B 113 ALA B 135 1 23
HELIX 18 AB9 GLY B 137 MET B 162 1 26
HELIX 19 AC1 ASN B 166 ILE B 183 1 18
HELIX 20 AC2 SER B 186 LEU B 205 1 20
HELIX 21 AC3 HIS B 206 LEU B 208 5 3
HELIX 22 AC4 SER B 209 THR B 231 1 23
HELIX 23 AC5 GLU E 2 ALA E 16 1 15
HELIX 24 AC6 ARG E 18 GLU E 31 1 14
HELIX 25 AC7 SER E 37 SER E 69 1 33
HELIX 26 AC8 PRO E 79 HIS E 106 1 28
HELIX 27 AC9 ASP E 113 ALA E 135 1 23
HELIX 28 AD1 GLY E 137 MET E 162 1 26
HELIX 29 AD2 ASN E 166 ILE E 183 1 18
HELIX 30 AD3 SER E 186 LEU E 205 1 20
HELIX 31 AD4 HIS E 206 LEU E 208 5 3
HELIX 32 AD5 SER E 209 THR E 231 1 23
HELIX 33 AD6 PRO F -1 ALA F 16 1 18
HELIX 34 AD7 ARG F 18 GLU F 31 1 14
HELIX 35 AD8 SER F 37 SER F 69 1 33
HELIX 36 AD9 GLY F 78 HIS F 106 1 29
HELIX 37 AE1 HIS F 106 ALA F 111 1 6
HELIX 38 AE2 ASP F 113 ALA F 135 1 23
HELIX 39 AE3 GLY F 137 MET F 162 1 26
HELIX 40 AE4 ASN F 166 ILE F 183 1 18
HELIX 41 AE5 SER F 186 ASP F 204 1 19
HELIX 42 AE6 LEU F 205 LEU F 208 5 4
HELIX 43 AE7 SER F 212 THR F 231 1 20
LINK C ALA C 15 N SEP C 16 1555 1555 1.32
LINK C SEP C 16 N ALA C 17 1555 1555 1.32
LINK C ALA D 15 N SEP D 16 1555 1555 1.32
LINK C SEP D 16 N ALA D 17 1555 1555 1.33
LINK C ALA G 15 N SEP G 16 1555 1555 1.33
LINK C SEP G 16 N ALA G 17 1555 1555 1.35
LINK C ALA H 15 N SEP H 16 1555 1555 1.32
LINK C SEP H 16 N ALA H 17 1555 1555 1.34
CISPEP 1 ASN A 70 GLU A 71 0 -2.55
CISPEP 2 ALA A 77 GLY A 78 0 1.19
CISPEP 3 ALA B 111 GLY B 112 0 -1.57
SITE 1 AC1 4 ASP A 97 LEU A 131 ASP A 139 ILE A 143
SITE 1 AC2 4 ASP B 97 LEU B 131 ASP B 139 ILE B 143
SITE 1 AC3 4 ASP E 97 LEU E 131 ASP E 139 ILE E 143
SITE 1 AC4 4 ASP F 97 LEU F 131 ASP F 139 ILE F 143
CRYST1 55.610 104.010 123.070 90.00 93.89 90.00 P 1 21 1 8
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 0.017982 0.000000 0.001223 0.00000
SCALE2 0.000000 0.009614 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008144 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
