Header list of 1i6z.pdb file
Complete list - b 23 2 Bytes
HEADER CHAPERONE 06-MAR-01 1I6Z
TITLE BAG DOMAIN OF BAG1 COCHAPERONE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: BAG-FAMILY MOLECULAR CHAPERONE REGULATOR-1;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: BAG DOMAIN;
COMPND 5 SYNONYM: BCL-2 BINDING ATHANOGENE-1, BAG-1;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 3 ORGANISM_COMMON: HOUSE MOUSE;
SOURCE 4 ORGANISM_TAXID: 10090;
SOURCE 5 GENE: BAG1;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PGEX-3X
KEYWDS TRIPLE HELIX BUNDLE, CHAPERONE
EXPDTA SOLUTION NMR
NUMMDL 25
AUTHOR K.BRIKNAROVA,S.TAKAYAMA,L.BRIVE,M.L.HAVERT,D.A.KNEE,J.VELASCO,
AUTHOR 2 S.HOMMA,E.CABEZAS,J.STUART,D.W.HOYT,A.C.SATTERTHWAIT,M.LLINAS,
AUTHOR 3 J.C.REED,K.R.ELY
REVDAT 3 23-FEB-22 1I6Z 1 REMARK SEQADV
REVDAT 2 24-FEB-09 1I6Z 1 VERSN
REVDAT 1 06-SEP-01 1I6Z 0
JRNL AUTH K.BRIKNAROVA,S.TAKAYAMA,L.BRIVE,M.L.HAVERT,D.A.KNEE,
JRNL AUTH 2 J.VELASCO,S.HOMMA,E.CABEZAS,J.STUART,D.W.HOYT,
JRNL AUTH 3 A.C.SATTERTHWAIT,M.LLINAS,J.C.REED,K.R.ELY
JRNL TITL STRUCTURAL ANALYSIS OF BAG1 COCHAPERONE AND ITS INTERACTIONS
JRNL TITL 2 WITH HSC70 HEAT SHOCK PROTEIN.
JRNL REF NAT.STRUCT.BIOL. V. 8 349 2001
JRNL REFN ISSN 1072-8368
JRNL PMID 11276257
JRNL DOI 10.1038/86236
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : VNMR, CNS 1.0
REMARK 3 AUTHORS : VARIAN (VNMR), BRUNGER (CNS)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1I6Z COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 08-MAR-01.
REMARK 100 THE DEPOSITION ID IS D_1000012982.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 310
REMARK 210 PH : 7.2
REMARK 210 IONIC STRENGTH : 10MM POTASSIUM PHOSPHATE, 25MM
REMARK 210 KCL
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 2MM BAG1 U-15N; 10MM POTASSIUM
REMARK 210 PHOSPHATE BUFFER, PH 7.2; 25MM
REMARK 210 KCL; 1MM EDTA; 1MM DTT; 0.02%
REMARK 210 NAN3; 90%H2O, 10%D2O; 2MM BAG1 U-
REMARK 210 15N,13C; 10MM POTASSIUM
REMARK 210 PHOSPHATE BUFFER, PH 7.2; 25MM
REMARK 210 KCL; 1MM EDTA; 1MM DTT; 0.02%
REMARK 210 NAN3; 90%H2O, 10%D2O; 2MM BAG1 U-
REMARK 210 15N,13C; 10MM POTASSIUM
REMARK 210 PHOSPHATE BUFFER, PH 7.2; 25MM
REMARK 210 KCL; 1MM EDTA; 1MM DTT; 0.02%
REMARK 210 NAN3; 100%D2O; 2MM BAG1 U-15N,2H;
REMARK 210 10MM POTASSIUM PHOSPHATE BUFFER,
REMARK 210 PH 7.2; 25MM KCL; 1MM EDTA; 1MM
REMARK 210 DTT; 0.02% NAN3; 90%H2O, 10%D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY; 4D_13C
REMARK 210 -SEPARATED_NOESY; 4D_15N-
REMARK 210 SEPARATED_NOESY; 3D_13C/15N-
REMARK 210 SEPARATED_NOESY; CBCA(CO)NH;
REMARK 210 HNCACB; C(CO)NH; H(CCO)NH; HCCH-
REMARK 210 TOCSY; HNCO
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 600 MHZ; 750 MHZ
REMARK 210 SPECTROMETER MODEL : AVANCE; UNITY; INOVA; UNITYPLUS
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER; VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : FELIX 98.0, CNS 1.0
REMARK 210 METHOD USED : TORSION ANGLE DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 25
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 25
REMARK 210 CONFORMERS, SELECTION CRITERIA : ALL CALCULATED STRUCTURES
REMARK 210 SUBMITTED
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: MONOMERIC
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 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 O GLN A 201 H GLN A 205 1.59
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 SER A 86 83.57 -162.80
REMARK 500 1 MET A 90 -40.97 -168.97
REMARK 500 1 LEU A 91 -34.52 -160.86
REMARK 500 1 ILE A 92 64.52 73.06
REMARK 500 1 GLU A 94 118.41 61.40
REMARK 500 1 LYS A 95 51.25 -142.22
REMARK 500 1 SER A 96 179.89 62.32
REMARK 500 1 ASN A 97 66.42 -110.89
REMARK 500 1 PRO A 98 -78.25 -61.83
REMARK 500 1 PHE A 135 -48.53 -178.15
REMARK 500 1 PRO A 172 -168.95 -70.76
REMARK 500 1 GLU A 173 32.43 -98.88
REMARK 500 1 PHE A 175 87.11 -69.66
REMARK 500 1 SER A 212 -52.59 -121.31
REMARK 500 1 THR A 213 -176.81 51.12
REMARK 500 1 ALA A 218 -47.34 -147.32
REMARK 500 2 SER A 86 -62.68 -171.98
REMARK 500 2 PHE A 89 153.29 61.58
REMARK 500 2 SER A 96 -179.09 64.63
REMARK 500 2 PRO A 98 -82.93 -69.58
REMARK 500 2 GLN A 133 -42.09 -29.68
REMARK 500 2 PHE A 135 39.59 -171.16
REMARK 500 2 GLN A 174 -56.02 -176.98
REMARK 500 2 LEU A 215 30.79 -162.36
REMARK 500 2 LEU A 217 -55.11 -145.18
REMARK 500 3 LEU A 91 59.92 -171.99
REMARK 500 3 GLU A 94 164.30 60.61
REMARK 500 3 PRO A 98 -70.23 -91.14
REMARK 500 3 GLU A 173 -168.61 -77.71
REMARK 500 3 GLN A 174 -58.74 78.71
REMARK 500 3 PHE A 175 89.06 -52.37
REMARK 500 3 ALA A 216 -57.12 -136.98
REMARK 500 3 LEU A 217 -43.28 -174.41
REMARK 500 4 SER A 86 153.61 61.18
REMARK 500 4 GLU A 88 -46.25 -132.20
REMARK 500 4 SER A 96 131.90 65.38
REMARK 500 4 PRO A 172 -168.59 -72.26
REMARK 500 4 GLU A 173 47.15 -94.79
REMARK 500 4 GLN A 211 -38.73 170.08
REMARK 500 4 SER A 212 142.52 60.69
REMARK 500 4 ASN A 214 94.51 179.63
REMARK 500 4 LEU A 215 -164.56 -163.64
REMARK 500 4 ALA A 216 159.85 68.87
REMARK 500 5 PRO A 87 99.75 -68.22
REMARK 500 5 GLU A 88 147.92 62.70
REMARK 500 5 LEU A 91 95.70 67.23
REMARK 500 5 LYS A 95 -76.70 -128.60
REMARK 500 5 ASN A 97 118.18 62.40
REMARK 500 5 PHE A 135 -61.10 -170.66
REMARK 500 5 GLU A 173 71.14 64.35
REMARK 500
REMARK 500 THIS ENTRY HAS 281 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1I6Z A 90 219 UNP Q60739 BAG1_MOUSE 226 355
SEQADV 1I6Z GLY A 85 UNP Q60739 CLONING ARTIFACT
SEQADV 1I6Z SER A 86 UNP Q60739 CLONING ARTIFACT
SEQADV 1I6Z PRO A 87 UNP Q60739 CLONING ARTIFACT
SEQADV 1I6Z GLU A 88 UNP Q60739 CLONING ARTIFACT
SEQADV 1I6Z PHE A 89 UNP Q60739 CLONING ARTIFACT
SEQRES 1 A 135 GLY SER PRO GLU PHE MET LEU ILE GLY GLU LYS SER ASN
SEQRES 2 A 135 PRO GLU GLU GLU VAL GLU LEU LYS LYS LEU LYS ASP LEU
SEQRES 3 A 135 GLU VAL SER ALA GLU LYS ILE ALA ASN HIS LEU GLN GLU
SEQRES 4 A 135 LEU ASN LYS GLU LEU SER GLY ILE GLN GLN GLY PHE LEU
SEQRES 5 A 135 ALA LYS GLU LEU GLN ALA GLU ALA LEU CYS LYS LEU ASP
SEQRES 6 A 135 ARG LYS VAL LYS ALA THR ILE GLU GLN PHE MET LYS ILE
SEQRES 7 A 135 LEU GLU GLU ILE ASP THR MET VAL LEU PRO GLU GLN PHE
SEQRES 8 A 135 LYS ASP SER ARG LEU LYS ARG LYS ASN LEU VAL LYS LYS
SEQRES 9 A 135 VAL GLN VAL PHE LEU ALA GLU CYS ASP THR VAL GLU GLN
SEQRES 10 A 135 TYR ILE CYS GLN GLU THR GLU ARG LEU GLN SER THR ASN
SEQRES 11 A 135 LEU ALA LEU ALA GLU
HELIX 1 1 ASN A 97 GLN A 133 1 37
HELIX 2 2 ALA A 137 THR A 168 1 32
HELIX 3 3 PHE A 175 GLN A 211 1 37
CRYST1 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 - b 23 2 Bytes