Header list of 1m25.pdb file
Complete list - 23 20 Bytes
HEADER UNKNOWN FUNCTION 21-JUN-02 1M25
TITLE STRUCTURE OF SYNTHETIC 26-MER PEPTIDE CONTAINING 145-169 SHEEP PRION
TITLE 2 PROTEIN SEGMENT AND C-TERMINAL CYSTEINE IN TFE SOLUTION
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: MAJOR PRION PROTEIN;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: RESIDUES 145-169;
COMPND 5 SYNONYM: PRP;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 SYNTHETIC: YES;
SOURCE 3 OTHER_DETAILS: THIS PEPTIDE WAS CHEMICALLY SYNTHESIZED. EXCEPT FOR
SOURCE 4 THE C-TERMINAL CYSTEINE, THIS SEQUENCE OCCURS NATURALLY IN OVIS
SOURCE 5 ARIES (SHEEP).
KEYWDS HELIX, PRION, TFE, UNKNOWN FUNCTION
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR S.MEGY,G.BERTHO,S.A.KOZIN,G.COADOU,P.DEBEY,G.H.HOA,J.-P.GIRAULT
REVDAT 4 23-FEB-22 1M25 1 REMARK SEQADV
REVDAT 3 24-FEB-09 1M25 1 VERSN
REVDAT 2 15-MAR-05 1M25 1 JRNL
REVDAT 1 17-JUL-02 1M25 0
JRNL AUTH S.MEGY,G.BERTHO,S.A.KOZIN,P.DEBEY,G.H.HOA,J.-P.GIRAULT
JRNL TITL POSSIBLE ROLE OF REGION 152-156 IN THE STRUCTURAL DUALITY OF
JRNL TITL 2 A PEPTIDE FRAGMENT FROM SHEEP PRION PROTEIN
JRNL REF PROTEIN SCI. V. 13 3151 2004
JRNL REFN ISSN 0961-8368
JRNL PMID 15537751
JRNL DOI 10.1110/PS.04745004
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH S.A.KOZIN,G.BERTHO,A.K.MAZUR,H.RABESONA,J.-P.GIRAULT,
REMARK 1 AUTH 2 T.HAERTLE,M.TAKAHASHI,P.DEBEY,G.H.HOA
REMARK 1 TITL SHEEP PRION PROTEIN SYNTHETIC PEPTIDE SPANNING HELIX 1 AND
REMARK 1 TITL 2 BETA-STRAND 2 (RESIDUES 142-166) SHOWS BETA-HAIRPIN
REMARK 1 TITL 3 STRUCTURE IN SOLUTION
REMARK 1 REF J.BIOL.CHEM. V. 276 46364 2001
REMARK 1 REFN ISSN 0021-9258
REMARK 1 DOI 10.1074/JBC.M108014200
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : XWINNMR 2.1, CNS 0.9
REMARK 3 AUTHORS : BRUKER (XWINNMR), BRUNGER (CNS)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: THE STRUCTURES ARE BASED ON A TOTAL OF
REMARK 3 252 INTERRESIDUAL NOE-DERIVED DISTANCE CONSTRAINTS, 22 DIHEDRAL
REMARK 3 ANGLE RESTRAINTS, 25 CSI RESTRAINTS FROM HA, CA, CB.
REMARK 4
REMARK 4 1M25 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 28-JUN-02.
REMARK 100 THE DEPOSITION ID IS D_1000016503.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 278
REMARK 210 PH : 6.5
REMARK 210 IONIC STRENGTH : 1MM
REMARK 210 PRESSURE : 1 ATM
REMARK 210 SAMPLE CONTENTS : 4.5MM
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ
REMARK 210 SPECTROMETER MODEL : AMX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : CNS 0.9
REMARK 210 METHOD USED : SIMULATED ANNEALING USING
REMARK 210 TORSION ANGLE DYNAMICS AS
REMARK 210 IMPLEMENTED IN THE PROGRAM CNS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 200
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : BACK CALCULATED DATA AGREE WITH
REMARK 210 EXPERIMENTAL NOESY SPECTRUM,
REMARK 210 STRUCTURES WITH THE LOWEST ENERGY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 2
REMARK 210
REMARK 210 REMARK: THIS STRUCTURE WAS DETERMINED USING STANDARD 2D
REMARK 210 HOMONUCLEAR TECHNIQUES.
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 ASN A 18 H VAL A 20 1.24
REMARK 500 O ASN A 12 HD1 TYR A 16 1.31
REMARK 500 O TYR A 9 H ASN A 12 1.54
REMARK 500 O ASN A 2 H ASP A 6 1.57
REMARK 500 O ASP A 6 H ARG A 10 1.60
REMARK 500 O TYR A 14 OD1 ASN A 18 2.06
REMARK 500 O ASN A 12 CD1 TYR A 16 2.10
REMARK 500 O TYR A 21 N ARG A 23 2.14
REMARK 500 O ASN A 18 N VAL A 20 2.17
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 3 TYR A 9 CB - CG - CD1 ANGL. DEV. = -3.8 DEGREES
REMARK 500 5 TYR A 9 CB - CG - CD1 ANGL. DEV. = -3.6 DEGREES
REMARK 500 13 TYR A 9 CB - CG - CD1 ANGL. DEV. = -3.7 DEGREES
REMARK 500 17 TYR A 9 CB - CG - CD1 ANGL. DEV. = -3.6 DEGREES
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 ASP A 3 -6.94 -59.14
REMARK 500 1 GLU A 11 2.48 -65.28
REMARK 500 1 TYR A 16 -134.97 -75.97
REMARK 500 1 PRO A 17 71.76 -68.52
REMARK 500 1 GLN A 19 13.02 -28.03
REMARK 500 1 VAL A 20 -30.65 174.89
REMARK 500 1 TYR A 22 14.15 41.96
REMARK 500 1 ARG A 23 -48.32 96.75
REMARK 500 2 GLU A 11 6.82 -66.81
REMARK 500 2 TYR A 16 -149.04 -83.16
REMARK 500 2 GLN A 19 1.28 -26.73
REMARK 500 2 VAL A 20 -28.33 -175.11
REMARK 500 2 TYR A 22 17.92 44.04
REMARK 500 2 ARG A 23 -53.62 99.09
REMARK 500 3 GLU A 11 2.08 -66.21
REMARK 500 3 TYR A 16 -131.84 -75.46
REMARK 500 3 PRO A 17 67.96 -66.74
REMARK 500 3 GLN A 19 11.48 -28.03
REMARK 500 3 VAL A 20 -29.90 176.90
REMARK 500 3 TYR A 22 14.96 41.09
REMARK 500 3 ARG A 23 -49.60 96.96
REMARK 500 4 GLU A 11 8.10 -68.24
REMARK 500 4 TYR A 16 -130.50 -77.08
REMARK 500 4 PRO A 17 66.43 -65.89
REMARK 500 4 GLN A 19 12.51 -28.48
REMARK 500 4 VAL A 20 -31.52 175.39
REMARK 500 4 TYR A 22 14.92 41.94
REMARK 500 4 ARG A 23 -46.32 95.80
REMARK 500 5 TYR A 16 -144.44 -82.08
REMARK 500 5 PRO A 17 73.50 -67.00
REMARK 500 5 GLN A 19 1.80 -27.81
REMARK 500 5 VAL A 20 -28.89 -176.56
REMARK 500 5 TYR A 22 13.01 39.63
REMARK 500 5 ARG A 23 -41.67 93.73
REMARK 500 6 ASN A 2 -39.91 -160.64
REMARK 500 6 ASP A 3 -9.01 -57.54
REMARK 500 6 GLU A 11 2.74 -66.35
REMARK 500 6 TYR A 16 -135.70 -73.10
REMARK 500 6 PRO A 17 71.03 -65.48
REMARK 500 6 GLN A 19 9.72 -27.65
REMARK 500 6 VAL A 20 -29.26 178.43
REMARK 500 6 TYR A 22 14.91 42.04
REMARK 500 6 ARG A 23 -45.35 95.13
REMARK 500 7 ASP A 3 -9.53 -57.61
REMARK 500 7 GLU A 11 7.32 -67.28
REMARK 500 7 TYR A 16 -140.36 -70.91
REMARK 500 7 PRO A 17 75.05 -69.56
REMARK 500 7 GLN A 19 3.69 -27.31
REMARK 500 7 VAL A 20 -28.73 -177.19
REMARK 500 7 TYR A 22 15.57 42.74
REMARK 500
REMARK 500 THIS ENTRY HAS 143 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1G04 RELATED DB: PDB
REMARK 900 STRUCTURE OF THE SYNTHETIC 26-MER PEPTIDE CONTAINING 145-169 SHEEP
REMARK 900 PRION PROTEIN SEGMENT IN WATER SOLUTION
REMARK 900 RELATED ID: 4010 RELATED DB: BMRB
REMARK 900 NMR DATA FOR THE SYNTHETIC 26-MER PEPTIDE CONTAINING 145-169 SHEEP
REMARK 900 PRION PROTEIN SEGMENT IN WATER SOLUTION
DBREF 1M25 A 1 25 UNP P23907 PRIO_SHEEP 145 169
SEQADV 1M25 CYS A 26 UNP P23907 INSERTION
SEQRES 1 A 26 GLY ASN ASP TYR GLU ASP ARG TYR TYR ARG GLU ASN MET
SEQRES 2 A 26 TYR ARG TYR PRO ASN GLN VAL TYR TYR ARG PRO VAL CYS
HELIX 1 1 ASN A 2 GLU A 11 1 10
HELIX 2 2 ASN A 12 ARG A 15 5 4
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 - 23 20 Bytes