Header list of 1m62.pdb file
Complete list - b 23 2 Bytes
HEADER CHAPERONE 11-JUL-02 1M62
TITLE SOLUTION STRUCTURE OF THE BAG DOMAIN FROM BAG4/SODD
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: BAG-FAMILY MOLECULAR CHAPERONE REGULATOR-4;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: BAG DOMAIN (RESIDUES 371-457);
COMPND 5 SYNONYM: SILENCER OF DEATH DOMAINS;
COMPND 6 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: BAG4/SODD;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PGEX4T-1
KEYWDS BAG DOMAIN, BAG4, SODD, SILENCER OF DEATH DOMAINS, HSP70/HSC70 CO-
KEYWDS 2 CHAPERONE, CHAPERONE
EXPDTA SOLUTION NMR
NUMMDL 25
AUTHOR K.BRIKNAROVA,S.TAKAYAMA,S.HOMMA,K.BAKER,E.CABEZAS,D.W.HOYT,Z.LI,
AUTHOR 2 A.C.SATTERTHWAIT,K.R.ELY
REVDAT 4 23-FEB-22 1M62 1 REMARK SEQADV
REVDAT 3 24-FEB-09 1M62 1 VERSN
REVDAT 2 15-MAR-05 1M62 1 KEYWDS JRNL REMARK
REVDAT 1 24-JUL-02 1M62 0
JRNL AUTH K.BRIKNAROVA,S.TAKAYAMA,S.HOMMA,K.BAKER,E.CABEZAS,D.W.HOYT,
JRNL AUTH 2 Z.LI,A.C.SATTERTHWAIT,K.R.ELY
JRNL TITL BAG4/SODD PROTEIN CONTAINS A SHORT BAG DOMAIN.
JRNL REF J.BIOL.CHEM. V. 277 31172 2002
JRNL REFN ISSN 0021-9258
JRNL PMID 12058034
JRNL DOI 10.1074/JBC.M202792200
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : VNMR 6.1C, CNS 1.0
REMARK 3 AUTHORS : VARIAN INC. (VNMR), BRUNGER ET AL. (CNS)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1M62 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 12-JUL-02.
REMARK 100 THE DEPOSITION ID IS D_1000016643.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 303
REMARK 210 PH : 7.2
REMARK 210 IONIC STRENGTH : 0.12
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 1.5 MM BAG4 BD U-15N 13C, 10 MM
REMARK 210 POTASSIUM PHOSPHATE BUFFER PH
REMARK 210 7.2, 100 MM KCL, 1 MM DTT, 1 MM
REMARK 210 EDTA; 1.5 MM BAG4 BD U-15N, 10
REMARK 210 MM POTASSIUM PHOSPHATE BUFFER PH
REMARK 210 7.2, 100 MM KCL, 1 MM DTT, 1 MM
REMARK 210 EDTA
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D 13C/15N-SEPARATED NOESY;
REMARK 210 3D_15N-SEPARATED_NOESY; 3D
REMARK 210 CBCA(CO)NH; 3D HNCACB; 3D H(CCO)
REMARK 210 NH; 3D C(CO)NH; 3D HNCO
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 600 MHZ; 750 MHZ
REMARK 210 SPECTROMETER MODEL : UNITYPLUS; INOVA
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : FELIX 2000, CNS 1.0
REMARK 210 METHOD USED : TORSION ANGLE DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 28
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 25
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LEAST
REMARK 210 RESTRAINT VIOLATIONS,STRUCTURES
REMARK 210 WITH THE 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: 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
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 GLU A 374 172.74 55.91
REMARK 500 1 THR A 376 104.73 61.90
REMARK 500 1 PRO A 377 -174.90 -52.39
REMARK 500 1 PHE A 400 112.55 -27.42
REMARK 500 1 THR A 428 -167.98 45.47
REMARK 500 2 SER A 372 -61.62 -178.98
REMARK 500 2 PHE A 375 90.39 62.33
REMARK 500 2 PRO A 377 179.84 -58.60
REMARK 500 2 PHE A 400 142.68 58.92
REMARK 500 2 ASP A 424 30.95 -98.81
REMARK 500 2 THR A 428 -174.65 55.89
REMARK 500 2 GLN A 431 92.76 -60.17
REMARK 500 3 PHE A 375 -79.90 63.27
REMARK 500 3 PRO A 377 170.12 -49.98
REMARK 500 3 PHE A 400 113.11 -24.30
REMARK 500 4 PRO A 378 -77.29 -48.29
REMARK 500 4 PHE A 400 109.12 -4.71
REMARK 500 4 THR A 428 -72.69 -122.71
REMARK 500 4 GLN A 431 108.80 -160.21
REMARK 500 5 PHE A 375 173.86 60.81
REMARK 500 5 PRO A 377 -175.52 -53.19
REMARK 500 5 THR A 428 126.15 -178.48
REMARK 500 6 SER A 372 -61.78 -178.50
REMARK 500 6 GLU A 374 -51.52 -159.54
REMARK 500 6 PRO A 377 172.53 -56.85
REMARK 500 6 PHE A 400 107.83 21.96
REMARK 500 6 SER A 425 35.38 -95.30
REMARK 500 7 PRO A 373 -177.21 -67.33
REMARK 500 7 GLU A 374 125.08 63.62
REMARK 500 7 PRO A 377 -177.23 -51.46
REMARK 500 7 PHE A 400 159.11 56.13
REMARK 500 7 VAL A 401 20.49 -142.26
REMARK 500 7 THR A 428 -45.84 -156.67
REMARK 500 8 SER A 372 -61.67 -178.60
REMARK 500 8 PHE A 375 153.67 61.46
REMARK 500 8 GLU A 399 -69.03 -90.73
REMARK 500 8 PHE A 400 109.00 36.47
REMARK 500 9 THR A 376 136.50 69.16
REMARK 500 9 PRO A 377 -176.48 -57.07
REMARK 500 9 GLU A 399 -68.65 -91.78
REMARK 500 9 PHE A 400 -84.04 45.02
REMARK 500 10 PRO A 373 -167.93 -71.40
REMARK 500 10 GLU A 374 -42.53 -143.37
REMARK 500 10 PHE A 375 85.59 66.65
REMARK 500 10 THR A 376 137.89 71.58
REMARK 500 10 PRO A 378 -74.75 -91.97
REMARK 500 10 PHE A 400 -80.44 52.42
REMARK 500 10 THR A 428 157.62 61.69
REMARK 500 11 SER A 372 -61.40 -178.72
REMARK 500 11 PHE A 375 75.03 -109.94
REMARK 500
REMARK 500 THIS ENTRY HAS 120 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1I6Z RELATED DB: PDB
REMARK 900 SOLUTION STRUCTURE OF THE BAG DOMAIN FROM MURINE BAG1
REMARK 900 RELATED ID: 1HX1 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE BAG DOMAIN FROM HUMAN BAG1 IN COMPLEX WITH
REMARK 900 HSC70 ATPASE DOMAIN
DBREF 1M62 A 376 457 UNP O95429 BAG4_HUMAN 376 457
SEQADV 1M62 GLY A 371 UNP O95429 CLONING ARTIFACT
SEQADV 1M62 SER A 372 UNP O95429 CLONING ARTIFACT
SEQADV 1M62 PRO A 373 UNP O95429 CLONING ARTIFACT
SEQADV 1M62 GLU A 374 UNP O95429 CLONING ARTIFACT
SEQADV 1M62 PHE A 375 UNP O95429 CLONING ARTIFACT
SEQRES 1 A 87 GLY SER PRO GLU PHE THR PRO PRO SER ILE LYS LYS ILE
SEQRES 2 A 87 ILE HIS VAL LEU GLU LYS VAL GLN TYR LEU GLU GLN GLU
SEQRES 3 A 87 VAL GLU GLU PHE VAL GLY LYS LYS THR ASP LYS ALA TYR
SEQRES 4 A 87 TRP LEU LEU GLU GLU MET LEU THR LYS GLU LEU LEU GLU
SEQRES 5 A 87 LEU ASP SER VAL GLU THR GLY GLY GLN ASP SER VAL ARG
SEQRES 6 A 87 GLN ALA ARG LYS GLU ALA VAL CYS LYS ILE GLN ALA ILE
SEQRES 7 A 87 LEU GLU LYS LEU GLU LYS LYS GLY LEU
HELIX 1 1 SER A 379 PHE A 400 1 22
HELIX 2 2 ASP A 406 ASP A 424 1 19
HELIX 3 3 GLN A 431 LEU A 457 1 27
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 - b 23 2 Bytes