Header list of 1x53.pdb file
Complete list - r 2 2 Bytes
HEADER STRUCTURAL GENOMICS, UNKNOWN FUNCTION 15-MAY-05 1X53
TITLE THE SOLUTION STRUCTURE OF THE C-TERMINAL DOMAIN OF HUMAN ACTIVATOR OF
TITLE 2 90 KDA HEAT SHOCK PROTEIN ATPASE HOMOLOG 1
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ACTIVATOR OF 90 KDA HEAT SHOCK PROTEIN ATPASE HOMOLOG 1;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: C-TERMINAL DOMAIN;
COMPND 5 SYNONYM: AHA1, P38, HSPC322;
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: AHSA1;
SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: P040524-05;
SOURCE 8 OTHER_DETAILS: CELL-FREE PROTEIN SYNTHESIS
KEYWDS AHA1, HSP90, DUF704, C-TERMINAL DOMAIN, STRUCTURAL GENOMICS, NPPSFA,
KEYWDS 2 NATIONAL PROJECT ON PROTEIN STRUCTURAL AND FUNCTIONAL ANALYSES,
KEYWDS 3 RIKEN STRUCTURAL GENOMICS/PROTEOMICS INITIATIVE, RSGI, UNKNOWN
KEYWDS 4 FUNCTION
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR N.TOCHIO,S.KOSHIBA,M.INOUE,T.KIGAWA,S.YOKOYAMA,RIKEN STRUCTURAL
AUTHOR 2 GENOMICS/PROTEOMICS INITIATIVE (RSGI)
REVDAT 3 02-MAR-22 1X53 1 REMARK SEQADV
REVDAT 2 24-FEB-09 1X53 1 VERSN
REVDAT 1 15-NOV-05 1X53 0
JRNL AUTH N.TOCHIO,S.KOSHIBA,M.INOUE,T.KIGAWA,S.YOKOYAMA
JRNL TITL THE SOLUTION STRUCTURE OF THE C-TERMINAL DOMAIN OF HUMAN
JRNL TITL 2 ACTIVATOR OF 90 KDA HEAT SHOCK PROTEIN ATPASE HOMOLOG 1
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : XWINNMR 3.5, CYANA 2.0.17
REMARK 3 AUTHORS : BRUKER (XWINNMR), GUNTERT, P. (CYANA)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1X53 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 19-MAY-05.
REMARK 100 THE DEPOSITION ID IS D_1000024389.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 296
REMARK 210 PH : 7.0
REMARK 210 IONIC STRENGTH : 120MM
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 1.3MM AHA1 C-TERMINAL DOMAIN U
REMARK 210 -15N, 13C; 20MM D-TRIS HCL;
REMARK 210 100MM NACL; 1MM D-DTT; 0.02%
REMARK 210 NAN3; 10% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY; 3D_13C
REMARK 210 -SEPARATED_NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 900 MHZ
REMARK 210 SPECTROMETER MODEL : AVANCE
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NMRPIPE 20031121, NMRVIEW 5.0.4,
REMARK 210 KUJIRA 0.9044, CYANA 2.0.17
REMARK 210 METHOD USED : TORSION ANGLE DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : TARGET FUNCTION, STRUCTURES WITH
REMARK 210 THE LEAST RESTRAINT VIOLATIONS
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: 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 LEU A 20 39.54 -80.55
REMARK 500 1 PRO A 43 92.43 -48.02
REMARK 500 1 ALA A 48 95.89 -61.20
REMARK 500 1 ASP A 49 145.29 -174.78
REMARK 500 1 ARG A 50 97.11 -59.80
REMARK 500 1 GLU A 71 48.49 30.33
REMARK 500 1 LYS A 72 -59.42 -126.29
REMARK 500 1 PRO A 84 176.87 -50.85
REMARK 500 1 ASN A 99 49.79 73.32
REMARK 500 1 THR A 119 -70.31 -53.88
REMARK 500 1 TRP A 123 -67.63 -93.28
REMARK 500 1 PHE A 128 -67.42 -93.35
REMARK 500 1 GLU A 129 -33.06 -34.83
REMARK 500 1 SER A 144 42.79 -99.83
REMARK 500 2 ILE A 13 72.29 -119.61
REMARK 500 2 LEU A 20 38.86 -81.76
REMARK 500 2 PRO A 43 93.31 -47.95
REMARK 500 2 ALA A 48 95.96 -61.73
REMARK 500 2 ASP A 49 146.26 -174.98
REMARK 500 2 ARG A 50 98.46 -59.87
REMARK 500 2 GLU A 71 48.27 30.24
REMARK 500 2 LYS A 72 -58.62 -126.25
REMARK 500 2 ASN A 99 51.12 72.03
REMARK 500 2 THR A 119 -71.11 -49.06
REMARK 500 2 PHE A 128 -68.53 -92.79
REMARK 500 2 GLU A 129 -35.32 -33.77
REMARK 500 2 ALA A 139 75.81 -112.48
REMARK 500 2 SER A 140 141.93 -39.76
REMARK 500 3 LEU A 20 39.50 -81.25
REMARK 500 3 PRO A 43 91.04 -47.95
REMARK 500 3 ALA A 48 95.84 -62.22
REMARK 500 3 ASP A 49 146.53 -174.50
REMARK 500 3 ARG A 50 98.62 -59.62
REMARK 500 3 GLU A 71 48.81 28.69
REMARK 500 3 LYS A 72 -58.57 -126.85
REMARK 500 3 PRO A 84 171.87 -52.88
REMARK 500 3 THR A 119 -70.95 -49.82
REMARK 500 3 PHE A 128 -66.51 -93.10
REMARK 500 3 GLU A 129 -31.90 -34.65
REMARK 500 3 SER A 143 44.47 34.38
REMARK 500 4 LEU A 20 39.25 -80.64
REMARK 500 4 PRO A 43 90.35 -48.04
REMARK 500 4 ALA A 48 96.04 -62.60
REMARK 500 4 ASP A 49 146.76 -174.81
REMARK 500 4 ARG A 50 98.14 -60.31
REMARK 500 4 GLU A 71 47.63 29.99
REMARK 500 4 LYS A 72 -58.80 -125.34
REMARK 500 4 ASN A 99 49.67 73.45
REMARK 500 4 THR A 119 -70.44 -51.95
REMARK 500 4 TRP A 123 -67.85 -95.42
REMARK 500
REMARK 500 THIS ENTRY HAS 285 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: HSS001000725.1 RELATED DB: TARGETDB
DBREF 1X53 A 8 139 UNP O95433 AHSA1_HUMAN 204 335
SEQADV 1X53 GLY A 1 UNP O95433 CLONING ARTIFACT
SEQADV 1X53 SER A 2 UNP O95433 CLONING ARTIFACT
SEQADV 1X53 SER A 3 UNP O95433 CLONING ARTIFACT
SEQADV 1X53 GLY A 4 UNP O95433 CLONING ARTIFACT
SEQADV 1X53 SER A 5 UNP O95433 CLONING ARTIFACT
SEQADV 1X53 SER A 6 UNP O95433 CLONING ARTIFACT
SEQADV 1X53 GLY A 7 UNP O95433 CLONING ARTIFACT
SEQADV 1X53 SER A 140 UNP O95433 CLONING ARTIFACT
SEQADV 1X53 GLY A 141 UNP O95433 CLONING ARTIFACT
SEQADV 1X53 PRO A 142 UNP O95433 CLONING ARTIFACT
SEQADV 1X53 SER A 143 UNP O95433 CLONING ARTIFACT
SEQADV 1X53 SER A 144 UNP O95433 CLONING ARTIFACT
SEQADV 1X53 GLY A 145 UNP O95433 CLONING ARTIFACT
SEQRES 1 A 145 GLY SER SER GLY SER SER GLY ILE PRO THR CYS LYS ILE
SEQRES 2 A 145 THR LEU LYS GLU THR PHE LEU THR SER PRO GLU GLU LEU
SEQRES 3 A 145 TYR ARG VAL PHE THR THR GLN GLU LEU VAL GLN ALA PHE
SEQRES 4 A 145 THR HIS ALA PRO ALA THR LEU GLU ALA ASP ARG GLY GLY
SEQRES 5 A 145 LYS PHE HIS MET VAL ASP GLY ASN VAL SER GLY GLU PHE
SEQRES 6 A 145 THR ASP LEU VAL PRO GLU LYS HIS ILE VAL MET LYS TRP
SEQRES 7 A 145 ARG PHE LYS SER TRP PRO GLU GLY HIS PHE ALA THR ILE
SEQRES 8 A 145 THR LEU THR PHE ILE ASP LYS ASN GLY GLU THR GLU LEU
SEQRES 9 A 145 CYS MET GLU GLY ARG GLY ILE PRO ALA PRO GLU GLU GLU
SEQRES 10 A 145 ARG THR ARG GLN GLY TRP GLN ARG TYR TYR PHE GLU GLY
SEQRES 11 A 145 ILE LYS GLN THR PHE GLY TYR GLY ALA SER GLY PRO SER
SEQRES 12 A 145 SER GLY
HELIX 1 1 SER A 22 PHE A 30 1 9
HELIX 2 2 THR A 32 THR A 40 1 9
HELIX 3 3 ALA A 113 GLY A 122 1 10
HELIX 4 4 TYR A 127 PHE A 135 1 9
SHEET 1 A 5 THR A 10 PHE A 19 0
SHEET 2 A 5 THR A 102 PRO A 112 -1 O MET A 106 N LEU A 15
SHEET 3 A 5 ALA A 89 THR A 94 -1 N THR A 94 O CYS A 105
SHEET 4 A 5 HIS A 73 PHE A 80 -1 N MET A 76 O ILE A 91
SHEET 5 A 5 VAL A 61 SER A 62 -1 N SER A 62 O ARG A 79
SHEET 1 B 5 THR A 10 PHE A 19 0
SHEET 2 B 5 THR A 102 PRO A 112 -1 O MET A 106 N LEU A 15
SHEET 3 B 5 ALA A 89 THR A 94 -1 N THR A 94 O CYS A 105
SHEET 4 B 5 HIS A 73 PHE A 80 -1 N MET A 76 O ILE A 91
SHEET 5 B 5 PHE A 65 VAL A 69 -1 N THR A 66 O VAL A 75
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