Header list of 1hjm.pdb file
Complete list - 15 20 Bytes
HEADER PRION PROTEIN 27-FEB-03 1HJM
TITLE HUMAN PRION PROTEIN AT PH 7.0
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: MAJOR PRION PROTEIN PRECURSOR;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: GLOBULAR DOMAIN, RESIDUES 125-228;
COMPND 5 SYNONYM: PRP, PRP27-30, PRP33-35C, ASCR, CD230 ANTIGEN;
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 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS PRION PROTEIN, PRION, BRAIN, GLYCOPROTEIN, GPI-ANCHOR
EXPDTA SOLUTION NMR
MDLTYP MINIMIZED AVERAGE
AUTHOR L.CALZOLAI,R.ZAHN
REVDAT 4 15-JAN-20 1HJM 1 REMARK
REVDAT 3 24-FEB-09 1HJM 1 VERSN
REVDAT 2 11-SEP-03 1HJM 1 JRNL
REVDAT 1 03-JUL-03 1HJM 0
JRNL AUTH L.CALZOLAI,R.ZAHN
JRNL TITL INFLUENCE OF PH ON NMR STRUCTURE AND STABILITY OF THE HUMAN
JRNL TITL 2 PRION PROTEIN GLOBULAR DOMAIN
JRNL REF J.BIOL.CHEM. V. 278 35592 2003
JRNL REFN ISSN 0021-9258
JRNL PMID 12826672
JRNL DOI 10.1074/JBC.M303005200
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : OPALP
REMARK 3 AUTHORS : R.KORADI,M.BILLETER,P.GUNTERT
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1HJM COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 27-FEB-03.
REMARK 100 THE DEPOSITION ID IS D_1290012260.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 293
REMARK 210 PH : 7.0
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : NULL
REMARK 210 SAMPLE CONTENTS : NULL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : NULL
REMARK 210 SPECTROMETER FIELD STRENGTH : 750 MHZ
REMARK 210 SPECTROMETER MODEL : DRX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : DYANA
REMARK 210 METHOD USED : TORSION ANGLE DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 20
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 1
REMARK 210 CONFORMERS, SELECTION CRITERIA : LOWER TARGET FUNCTION
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL
REMARK 210
REMARK 210 REMARK: MORE SIMILAR TO MEAN STRUCTURE. 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 THR A 188 HG1 THR A 191 1.60
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 SER A 132 -163.07 -70.97
REMARK 500 MET A 134 37.90 -155.90
REMARK 500 SER A 135 -160.69 49.09
REMARK 500 TYR A 145 -72.39 -57.96
REMARK 500 HIS A 155 0.55 -65.61
REMARK 500 GLU A 168 -33.72 -159.70
REMARK 500 ASN A 171 178.68 174.02
REMARK 500 GLN A 172 -79.70 -70.61
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 ARG A 148 0.14 SIDE CHAIN
REMARK 500 TYR A 150 0.09 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1E1G RELATED DB: PDB
REMARK 900 HUMAN PRION PROTEIN VARIANT M166V
REMARK 900 RELATED ID: 1E1J RELATED DB: PDB
REMARK 900 HUMAN PRION PROTEIN VARIANT M166V
REMARK 900 RELATED ID: 1E1P RELATED DB: PDB
REMARK 900 HUMAN PRION PROTEIN VARIANT S170N
REMARK 900 RELATED ID: 1E1S RELATED DB: PDB
REMARK 900 HUMAN PRION PROTEIN VARIANT S170N
REMARK 900 RELATED ID: 1E1U RELATED DB: PDB
REMARK 900 HUMAN PRION PROTEIN VARIANT R220K
REMARK 900 RELATED ID: 1E1W RELATED DB: PDB
REMARK 900 HUMAN PRION PROTEIN VARIANT R220K
REMARK 900 RELATED ID: 1HJN RELATED DB: PDB
REMARK 900 HUMAN PRION PROTEIN AT PH 7.0
REMARK 900 RELATED ID: 5713 RELATED DB: BMRB
DBREF 1HJM A 125 228 UNP P04156 PRIO_HUMAN 125 228
SEQRES 1 A 104 LEU GLY GLY TYR MET LEU GLY SER ALA MET SER ARG PRO
SEQRES 2 A 104 ILE ILE HIS PHE GLY SER ASP TYR GLU ASP ARG TYR TYR
SEQRES 3 A 104 ARG GLU ASN MET HIS ARG TYR PRO ASN GLN VAL TYR TYR
SEQRES 4 A 104 ARG PRO MET ASP GLU TYR SER ASN GLN ASN ASN PHE VAL
SEQRES 5 A 104 HIS ASP CYS VAL ASN ILE THR ILE LYS GLN HIS THR VAL
SEQRES 6 A 104 THR THR THR THR LYS GLY GLU ASN PHE THR GLU THR ASP
SEQRES 7 A 104 VAL LYS MET MET GLU ARG VAL VAL GLU GLN MET CYS ILE
SEQRES 8 A 104 THR GLN TYR GLU ARG GLU SER GLN ALA TYR TYR GLN ARG
HELIX 1 1 SER A 143 ASN A 153 1 11
HELIX 2 2 MET A 154 TYR A 157 5 4
HELIX 3 3 ASN A 173 GLY A 195 1 23
HELIX 4 4 THR A 199 TYR A 226 1 28
SHEET 1 AA 2 MET A 129 LEU A 130 0
SHEET 2 AA 2 TYR A 162 TYR A 163 -1 O TYR A 163 N MET A 129
SSBOND 1 CYS A 179 CYS A 214 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
Complete list - 15 20 Bytes