Header list of 1q5l.pdb file
Complete list - r 2 2 Bytes
HEADER CHAPERONE 08-AUG-03 1Q5L
TITLE NMR STRUCTURE OF THE SUBSTRATE BINDING DOMAIN OF DNAK BOUND TO THE
TITLE 2 PEPTIDE NRLLLTG
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CHAPERONE PROTEIN DNAK;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: SUBSTRATE BINDING DOMAIN;
COMPND 5 SYNONYM: HEAT SHOCK PROTEIN 70, HEAT SHOCK 70 KDA PROTEIN, HSP70;
COMPND 6 ENGINEERED: YES;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: PEPTIDE NRLLLTG;
COMPND 9 CHAIN: B;
COMPND 10 FRAGMENT: SEQUENCE DATABASE RESIDUES 864-870;
COMPND 11 SYNONYM: ASN-ARG-LEU-LEU-LEU-THR-GLY PEPTIDE;
COMPND 12 ENGINEERED: YES;
COMPND 13 OTHER_DETAILS: IDENTIFIED AS A FAVORED BINDING SEQUENCE FROM PHAGE
COMPND 14 DISPLAY
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 562;
SOURCE 4 GENE: DNAK;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PET15B;
SOURCE 9 MOL_ID: 2;
SOURCE 10 SYNTHETIC: YES;
SOURCE 11 OTHER_DETAILS: THE PEPTIDE WAS CHEMICALLY SYNTHESIZED.
KEYWDS HSP70, CHAPERONE, HEAT SHOCK PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 15
AUTHOR S.Y.STEVENS,S.CAI,M.PELLECCHIA,E.R.ZUIDERWEG
REVDAT 3 02-MAR-22 1Q5L 1 REMARK SEQADV
REVDAT 2 24-FEB-09 1Q5L 1 VERSN
REVDAT 1 04-NOV-03 1Q5L 0
JRNL AUTH S.Y.STEVENS,S.CAI,M.PELLECCHIA,E.R.ZUIDERWEG
JRNL TITL THE SOLUTION STRUCTURE OF THE BACTERIAL HSP70 CHAPERONE
JRNL TITL 2 PROTEIN DOMAIN DNAK(393-507) IN COMPLEX WITH THE PEPTIDE
JRNL TITL 3 NRLLLTG.
JRNL REF PROTEIN SCI. V. 12 2588 2003
JRNL REFN ISSN 0961-8368
JRNL PMID 14573869
JRNL DOI 10.1110/PS.03269103
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : VNMR 2.6, ARIA/(CNS) 1.0
REMARK 3 AUTHORS : VARIAN (VNMR), NILGES (ARIA/(CNS))
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1Q5L COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 14-AUG-03.
REMARK 100 THE DEPOSITION ID IS D_1000019944.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 303
REMARK 210 PH : 7.4
REMARK 210 IONIC STRENGTH : 10 MM SODIUM PHOSPHATE
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 0.66 MM DNAK(393-507); 3.3 MM
REMARK 210 NRLLLTG; 10 MM SODIUM PHOSPHATE
REMARK 210 BUFFER, PH 7.4
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_13C-SEPARATED_NOESY; 3D_15N
REMARK 210 -SEPARATED_NOESY; H(C)CH_TOCSY;
REMARK 210 (H)CCH_TOCSY; 15N FILTERED/
REMARK 210 EDITED NOESY; 13C FILTERED/
REMARK 210 EDITED NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 800 MHZ; 500 MHZ
REMARK 210 SPECTROMETER MODEL : INOVA; AMX
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN; BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : VNMR 2.6, NMRPIPE, XEASY 3.2,
REMARK 210 ARIA/(CNS) 1.0
REMARK 210 METHOD USED : TORSION ANGLE DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 60
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 15
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH ACCEPTABLE
REMARK 210 COVALENT GEOMETRY,STRUCTURES
REMARK 210 WITH THE LEAST RESTRAINT
REMARK 210 VIOLATIONS,STRUCTURES WITH THE
REMARK 210 LOWEST ENERGY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
REMARK 210
REMARK 210 REMARK: NULL
REMARK 215
REMARK 215 NMR STUDY
REMARK 215 THE COORDINATES IN THIS ENTRY WERE GENERATED FROM SOLUTION
REMARK 215 NMR DATA. PROTEIN DATA BANK CONVENTIONS REQUIRE THAT
REMARK 215 CRYST1 AND SCALE RECORDS BE INCLUDED, BUT THE VALUES ON
REMARK 215 THESE RECORDS ARE MEANINGLESS.
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: DIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
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. (RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 465 SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465 MODELS 1-15
REMARK 465 RES C SSSEQI
REMARK 465 MET A 373
REMARK 465 GLY A 374
REMARK 465 SER A 375
REMARK 465 SER A 376
REMARK 465 HIS A 377
REMARK 465 HIS A 378
REMARK 465 HIS A 379
REMARK 465 HIS A 380
REMARK 465 HIS A 381
REMARK 465 HIS A 382
REMARK 465 GLY A 383
REMARK 465 LEU A 384
REMARK 465 VAL A 385
REMARK 465 PRO A 386
REMARK 465 ARG A 387
REMARK 465 GLY A 388
REMARK 465 SER A 389
REMARK 465 HIS A 390
REMARK 465 MET A 391
REMARK 465 VAL A 392
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
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
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 1 MET A 404 13.74 58.98
REMARK 500 1 LEU A 411 -59.45 -120.31
REMARK 500 1 ALA A 413 143.44 61.20
REMARK 500 1 LYS A 414 170.10 -57.13
REMARK 500 1 GLU A 430 90.09 62.54
REMARK 500 1 ASN A 432 55.07 78.39
REMARK 500 1 SER A 434 11.69 52.49
REMARK 500 1 ARG A 447 84.35 61.48
REMARK 500 1 ALA A 448 -137.71 -67.11
REMARK 500 1 ASP A 450 -28.68 -155.05
REMARK 500 1 ASN A 451 -165.53 -68.00
REMARK 500 1 LEU A 454 -70.36 -54.45
REMARK 500 1 ASN A 463 167.97 -49.42
REMARK 500 1 PRO A 464 99.55 -25.34
REMARK 500 1 PRO A 466 43.02 -76.85
REMARK 500 1 ARG A 467 156.38 62.39
REMARK 500 1 ASN A 492 -23.94 -175.77
REMARK 500 1 SER A 493 -14.56 -147.76
REMARK 500 1 ALA A 503 -78.38 -49.06
REMARK 500 1 SER A 504 90.25 -165.91
REMARK 500 1 SER A 505 -74.50 -129.44
REMARK 500 1 LEU B 903 -145.24 -98.23
REMARK 500 2 LEU A 397 147.94 -175.50
REMARK 500 2 LEU A 411 -59.60 -125.51
REMARK 500 2 LYS A 414 177.89 -56.03
REMARK 500 2 GLU A 430 97.67 63.80
REMARK 500 2 ASN A 432 39.98 71.25
REMARK 500 2 SER A 434 10.15 54.26
REMARK 500 2 ALA A 449 0.60 -68.40
REMARK 500 2 ASP A 450 69.98 -175.31
REMARK 500 2 LEU A 454 -71.33 -55.47
REMARK 500 2 ILE A 462 56.04 -143.14
REMARK 500 2 ASN A 463 168.13 -48.85
REMARK 500 2 PRO A 464 92.76 -29.40
REMARK 500 2 ALA A 465 112.47 -165.37
REMARK 500 2 ASN A 492 -21.51 -179.81
REMARK 500 2 SER A 493 -22.25 -157.91
REMARK 500 2 ARG B 902 -101.62 -125.65
REMARK 500 2 LEU B 903 87.05 53.55
REMARK 500 3 LEU A 411 -46.15 -131.34
REMARK 500 3 LYS A 414 173.42 -52.62
REMARK 500 3 PRO A 419 82.08 -69.91
REMARK 500 3 GLU A 430 79.27 74.94
REMARK 500 3 ASN A 432 57.97 74.29
REMARK 500 3 SER A 434 19.21 46.37
REMARK 500 3 ALA A 448 96.49 -68.18
REMARK 500 3 ASP A 450 38.50 -173.27
REMARK 500 3 LEU A 454 -70.99 -53.86
REMARK 500 3 ILE A 462 -5.03 -145.96
REMARK 500 3 ASN A 463 170.39 45.65
REMARK 500
REMARK 500 THIS ENTRY HAS 323 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1DG4 RELATED DB: PDB
REMARK 900 NMR STRUCTURE OF THE APO FORM OF THE SAME CONSTRUCT OF THE
REMARK 900 SUBSTRATE BINDING DOMAIN OF DNAK
REMARK 900 RELATED ID: 1DKX RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE SUBSTRATE BINDING DOMAIN OF DNAK BOUND TO
REMARK 900 THE PEPTIDE NRLLLTG
REMARK 900 RELATED ID: 1BPR RELATED DB: PDB
REMARK 900 NMR STRUCTURE OF THE SUBSTRATE BINDING DOMAIN BOUND
REMARK 900 INTRAMOLECULARLY TO ITS C-TERMINAL TAIL
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 THE REFERENCE FOR THE PEPTIDE IS
REMARK 999 GRAGEROV, A., ZENG, L., ZHAO, W., BURKHOLDER, W.,
REMARK 999 AND GOTTESMAN, M.E., SPECIFICITY OF DNAK-PEPTIDE BINDING.
REMARK 999 J.MOL. BIOL. (1994) 235, 848-854.
DBREF 1Q5L A 393 507 UNP P0A6Y8 DNAK_ECOLI 392 506
DBREF 1Q5L B 901 907 PDB 1Q5L 1Q5L 901 907
SEQADV 1Q5L MET A 373 UNP P0A6Y8 CLONING ARTIFACT
SEQADV 1Q5L GLY A 374 UNP P0A6Y8 CLONING ARTIFACT
SEQADV 1Q5L SER A 375 UNP P0A6Y8 CLONING ARTIFACT
SEQADV 1Q5L SER A 376 UNP P0A6Y8 CLONING ARTIFACT
SEQADV 1Q5L HIS A 377 UNP P0A6Y8 CLONING ARTIFACT
SEQADV 1Q5L HIS A 378 UNP P0A6Y8 CLONING ARTIFACT
SEQADV 1Q5L HIS A 379 UNP P0A6Y8 CLONING ARTIFACT
SEQADV 1Q5L HIS A 380 UNP P0A6Y8 CLONING ARTIFACT
SEQADV 1Q5L HIS A 381 UNP P0A6Y8 CLONING ARTIFACT
SEQADV 1Q5L HIS A 382 UNP P0A6Y8 CLONING ARTIFACT
SEQADV 1Q5L GLY A 383 UNP P0A6Y8 CLONING ARTIFACT
SEQADV 1Q5L LEU A 384 UNP P0A6Y8 CLONING ARTIFACT
SEQADV 1Q5L VAL A 385 UNP P0A6Y8 CLONING ARTIFACT
SEQADV 1Q5L PRO A 386 UNP P0A6Y8 CLONING ARTIFACT
SEQADV 1Q5L ARG A 387 UNP P0A6Y8 CLONING ARTIFACT
SEQADV 1Q5L GLY A 388 UNP P0A6Y8 CLONING ARTIFACT
SEQADV 1Q5L SER A 389 UNP P0A6Y8 CLONING ARTIFACT
SEQADV 1Q5L HIS A 390 UNP P0A6Y8 CLONING ARTIFACT
SEQADV 1Q5L MET A 391 UNP P0A6Y8 CLONING ARTIFACT
SEQADV 1Q5L VAL A 392 UNP P0A6Y8 CLONING ARTIFACT
SEQRES 1 A 135 MET GLY SER SER HIS HIS HIS HIS HIS HIS GLY LEU VAL
SEQRES 2 A 135 PRO ARG GLY SER HIS MET VAL ASP VAL THR PRO LEU SER
SEQRES 3 A 135 LEU GLY ILE GLU THR MET GLY GLY VAL MET THR THR LEU
SEQRES 4 A 135 ILE ALA LYS ASN THR THR ILE PRO THR LYS HIS SER GLN
SEQRES 5 A 135 VAL PHE SER THR ALA GLU ASP ASN GLN SER ALA VAL THR
SEQRES 6 A 135 ILE HIS VAL LEU GLN GLY GLU ARG LYS ARG ALA ALA ASP
SEQRES 7 A 135 ASN LYS SER LEU GLY GLN PHE ASN LEU ASP GLY ILE ASN
SEQRES 8 A 135 PRO ALA PRO ARG GLY MET PRO GLN ILE GLU VAL THR PHE
SEQRES 9 A 135 ASP ILE ASP ALA ASP GLY ILE LEU HIS VAL SER ALA LYS
SEQRES 10 A 135 ASP LYS ASN SER GLY LYS GLU GLN LYS ILE THR ILE LYS
SEQRES 11 A 135 ALA SER SER GLY LEU
SEQRES 1 B 7 ASN ARG LEU LEU LEU THR GLY
SHEET 1 A 4 VAL A 407 MET A 408 0
SHEET 2 A 4 ILE A 401 THR A 403 -1 N THR A 403 O VAL A 407
SHEET 3 A 4 THR A 437 GLN A 442 -1 O HIS A 439 N GLU A 402
SHEET 4 A 4 LYS A 452 ASN A 458 -1 O GLY A 455 N VAL A 440
SHEET 1 B 4 SER A 423 PHE A 426 0
SHEET 2 B 4 ILE A 472 ILE A 478 -1 O ILE A 472 N PHE A 426
SHEET 3 B 4 ILE A 483 ASP A 490 -1 O HIS A 485 N ASP A 477
SHEET 4 B 4 GLU A 496 LYS A 502 -1 O ILE A 501 N LEU A 484
CRYST1 1.000 1.000 1.000 90.00 90.00 90.00 P 1 1
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 1.000000 0.000000 0.000000 0.00000
SCALE2 0.000000 1.000000 0.000000 0.00000
SCALE3 0.000000 0.000000 1.000000 0.00000
MODEL 1
Complete list - r 2 2 Bytes