HEADER CHAPERONE 14-JAN-17 5WYO
TITLE SOLUTION STRUCTURE OF E.COLI HDEA
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ACID STRESS CHAPERONE HDEA;
COMPND 3 CHAIN: A, B;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI O157:H7;
SOURCE 3 ORGANISM_TAXID: 83334;
SOURCE 4 STRAIN: O157:H7;
SOURCE 5 GENE: HDEA, Z4922, ECS4390;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: VECTOR
KEYWDS PERIPLASMIC PROTEIN, CHAPERONE
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR C.YANG,Y.HU,C.JIN
REVDAT 2 14-JUN-23 5WYO 1 REMARK
REVDAT 1 22-NOV-17 5WYO 0
JRNL AUTH X.C.YU,C.YANG,J.DING,X.NIU,Y.HU,C.JIN
JRNL TITL CHARACTERIZATIONS OF THE INTERACTIONS BETWEEN ESCHERICHIA
JRNL TITL 2 COLI PERIPLASMIC CHAPERONE HDEA AND ITS NATIVE SUBSTRATES
JRNL TITL 3 DURING ACID STRESS
JRNL REF BIOCHEMISTRY V. 56 5748 2017
JRNL REFN ISSN 1520-4995
JRNL PMID 29016106
JRNL DOI 10.1021/ACS.BIOCHEM.7B00724
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : AMBER
REMARK 3 AUTHORS : CASE, DARDEN, CHEATHAM III, SIMMERLING, WANG,
REMARK 3 DUKE, LUO, ... AND KOLLMAN
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 5WYO COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 19-JAN-17.
REMARK 100 THE DEPOSITION ID IS D_1300002610.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 3.0
REMARK 210 IONIC STRENGTH : 180
REMARK 210 PRESSURE : 1 ATM
REMARK 210 SAMPLE CONTENTS : 2.0 MM [U-99% 13C; U-99% 15N]
REMARK 210 HDEA, 20 MM SODIUM CITRATE, 20
REMARK 210 MM SODIUM PHOSPHATE, 90% H2O/10%
REMARK 210 D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D 1H-15N HSQC; 3D HNCO; 3D
REMARK 210 HNCA; 3D CBCA(CO)NH; 3D HNCACB;
REMARK 210 3D HBHA(CO)NH; 3D HCCH-TOCSY; 3D
REMARK 210 HCCH-COSY; 3D 1H-15N NOESY; 3D
REMARK 210 1H-13C NOESY; 3D 13C/15N-
REMARK 210 FILTERED 13C-EDITED NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ; 700 MHZ; 800 MHZ
REMARK 210 SPECTROMETER MODEL : AVANCE III
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : CYANA, NMRVIEW
REMARK 210 METHOD USED : SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LOWEST
REMARK 210 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 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 LYS A 5 -69.07 56.46
REMARK 500 1 ALA A 6 -56.84 -153.04
REMARK 500 1 VAL A 13 2.24 -64.33
REMARK 500 1 SER A 15 -13.22 -142.55
REMARK 500 1 LEU A 50 155.00 64.49
REMARK 500 1 ASP A 51 62.22 -119.11
REMARK 500 1 PRO A 60 0.85 -68.48
REMARK 500 1 LYS A 75 -32.15 60.44
REMARK 500 1 LYS B 94 48.94 37.51
REMARK 500 1 ASN B 98 15.53 51.98
REMARK 500 1 LYS B 99 105.42 56.40
REMARK 500 1 SER B 104 -40.52 -142.05
REMARK 500 1 ALA B 125 -70.98 -96.72
REMARK 500 1 LYS B 131 -130.08 -150.66
REMARK 500 1 ASP B 132 -54.12 -157.07
REMARK 500 1 LEU B 139 144.36 60.47
REMARK 500 1 ASP B 140 44.44 -87.93
REMARK 500 1 LYS B 175 -61.82 -101.47
REMARK 500 2 ALA A 6 -115.40 45.35
REMARK 500 2 ASN A 9 -5.56 -147.57
REMARK 500 2 LYS A 42 -129.52 -141.41
REMARK 500 2 ASP A 43 -50.80 -161.87
REMARK 500 2 LEU A 50 112.13 62.78
REMARK 500 2 ASP A 51 54.07 -90.90
REMARK 500 2 PRO A 60 1.24 -69.40
REMARK 500 2 ASP A 88 15.30 54.57
REMARK 500 2 ASP B 97 -29.78 59.86
REMARK 500 2 PHE B 124 -57.57 -126.39
REMARK 500 2 LYS B 131 -122.97 -146.11
REMARK 500 2 ASP B 132 -79.31 -160.30
REMARK 500 3 LYS A 5 37.54 -77.48
REMARK 500 3 LYS A 10 92.69 40.24
REMARK 500 3 LYS A 11 60.71 -115.90
REMARK 500 3 VAL A 13 7.76 -63.50
REMARK 500 3 LYS A 42 -120.15 -156.13
REMARK 500 3 ASP A 43 -58.88 -161.18
REMARK 500 3 LEU A 50 110.01 66.64
REMARK 500 3 ASP A 51 59.83 -96.39
REMARK 500 3 PHE A 74 153.09 -48.28
REMARK 500 3 LYS A 75 -34.63 60.29
REMARK 500 3 ALA B 92 159.95 63.75
REMARK 500 3 GLN B 93 -154.21 -155.39
REMARK 500 3 LYS B 94 42.69 -73.99
REMARK 500 3 ALA B 95 90.60 58.35
REMARK 500 3 ALA B 96 -154.65 52.84
REMARK 500 3 ASN B 98 13.53 -149.76
REMARK 500 3 LYS B 131 -124.14 -154.16
REMARK 500 3 ASP B 132 -45.68 -163.66
REMARK 500 3 ASP B 140 48.98 -87.07
REMARK 500 4 ALA A 7 -81.96 56.97
REMARK 500
REMARK 500 THIS ENTRY HAS 281 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 36045 RELATED DB: BMRB
REMARK 900 SOLUTION STRUCTURE OF E.COLI HDEA
DBREF 5WYO A 1 89 UNP P0AET0 HDEA_ECO57 22 110
DBREF 5WYO B 90 178 UNP P0AET0 HDEA_ECO57 22 110
SEQRES 1 A 89 ALA ASP ALA GLN LYS ALA ALA ASP ASN LYS LYS PRO VAL
SEQRES 2 A 89 ASN SER TRP THR CYS GLU ASP PHE LEU ALA VAL ASP GLU
SEQRES 3 A 89 SER PHE GLN PRO THR ALA VAL GLY PHE ALA GLU ALA LEU
SEQRES 4 A 89 ASN ASN LYS ASP LYS PRO GLU ASP ALA VAL LEU ASP VAL
SEQRES 5 A 89 GLN GLY ILE ALA THR VAL THR PRO ALA ILE VAL GLN ALA
SEQRES 6 A 89 CYS THR GLN ASP LYS GLN ALA ASN PHE LYS ASP LYS VAL
SEQRES 7 A 89 LYS GLY GLU TRP ASP LYS ILE LYS LYS ASP MET
SEQRES 1 B 89 ALA ASP ALA GLN LYS ALA ALA ASP ASN LYS LYS PRO VAL
SEQRES 2 B 89 ASN SER TRP THR CYS GLU ASP PHE LEU ALA VAL ASP GLU
SEQRES 3 B 89 SER PHE GLN PRO THR ALA VAL GLY PHE ALA GLU ALA LEU
SEQRES 4 B 89 ASN ASN LYS ASP LYS PRO GLU ASP ALA VAL LEU ASP VAL
SEQRES 5 B 89 GLN GLY ILE ALA THR VAL THR PRO ALA ILE VAL GLN ALA
SEQRES 6 B 89 CYS THR GLN ASP LYS GLN ALA ASN PHE LYS ASP LYS VAL
SEQRES 7 B 89 LYS GLY GLU TRP ASP LYS ILE LYS LYS ASP MET
HELIX 1 AA1 THR A 17 LEU A 22 5 6
HELIX 2 AA2 PHE A 28 LEU A 39 1 12
HELIX 3 AA3 LYS A 44 ALA A 48 5 5
HELIX 4 AA4 ASP A 51 ASP A 69 1 19
HELIX 5 AA5 LYS A 75 LYS A 86 1 12
HELIX 6 AA6 THR B 106 LEU B 111 1 6
HELIX 7 AA7 PHE B 117 ASN B 130 1 14
HELIX 8 AA8 ASP B 140 ASP B 158 1 19
HELIX 9 AA9 ASN B 162 LYS B 175 1 14
SSBOND 1 CYS A 18 CYS A 66 1555 1555 2.05
SSBOND 2 CYS B 107 CYS B 155 1555 1555 2.05
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
(ATOM LINES ARE NOT SHOWN.)
END
