Header list of 1xyq.pdb file
Complete list - r 2 2 Bytes
HEADER UNKNOWN FUNCTION 10-NOV-04 1XYQ TITLE NMR STRUCTURE OF THE PIG PRION PROTEIN COMPND MOL_ID: 1; COMPND 2 MOLECULE: MAJOR PRION PROTEIN; COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: RESIDUES 121-231; COMPND 5 SYNONYM: PRP; COMPND 6 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: SUS SCROFA; SOURCE 3 ORGANISM_COMMON: PIG; SOURCE 4 ORGANISM_TAXID: 9823; SOURCE 5 GENE: PRNP; SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 511693; SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21 KEYWDS PRION, PRP, SCPRP, TSE, UNKNOWN FUNCTION EXPDTA SOLUTION NMR NUMMDL 20 AUTHOR D.A.LYSEK,C.SCHORN,T.HERRMANN,K.WUTHRICH REVDAT 5 02-MAR-22 1XYQ 1 REMARK REVDAT 4 24-FEB-09 1XYQ 1 VERSN REVDAT 3 25-JAN-05 1XYQ 1 JRNL REVDAT 2 11-JAN-05 1XYQ 1 AUTHOR JRNL REVDAT 1 04-JAN-05 1XYQ 0 JRNL AUTH D.A.LYSEK,C.SCHORN,L.G.NIVON,V.ESTEVE-MOYA,B.CHRISTEN, JRNL AUTH 2 L.CALZOLAI,C.VON SCHROETTER,F.FIORITO,T.HERRMANN,P.GUNTERT, JRNL AUTH 3 K.WUTHRICH JRNL TITL PRION PROTEIN NMR STRUCTURES OF CATS, DOGS, PIGS, AND SHEEP JRNL REF PROC.NATL.ACAD.SCI.USA V. 102 640 2005 JRNL REFN ISSN 0027-8424 JRNL PMID 15647367 JRNL DOI 10.1073/PNAS.0408937102 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : DYANA 6.2, CANDID 1.0 REMARK 3 AUTHORS : GNTERT (DYANA), HERRMANN (CANDID) REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 1XYQ COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 15-NOV-04. REMARK 100 THE DEPOSITION ID IS D_1000030912. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 293 REMARK 210 PH : 4.5 REMARK 210 IONIC STRENGTH : 10 REMARK 210 PRESSURE : AMBIENT REMARK 210 SAMPLE CONTENTS : 1MM PIG PRION PROTEIN, U-15N, REMARK 210 13C; 10MM ACETATE REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY; 3D_13C REMARK 210 -SEPARATED_NOESY REMARK 210 SPECTROMETER FIELD STRENGTH : 750 MHZ; 800 MHZ REMARK 210 SPECTROMETER MODEL : DRX; AVANCE REMARK 210 SPECTROMETER MANUFACTURER : BRUKER REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : NULL 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 REMARK 210 REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1 REMARK 210 REMARK 210 REMARK: THIS STRUCTURE WAS DETERMINED USING STANDARD 3D REMARK 210 HETERONUCLEAR 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: 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 1 TYR A 169 CB - CG - CD2 ANGL. DEV. = -3.6 DEGREES REMARK 500 1 ALA A 230 CB - CA - C ANGL. DEV. = 9.8 DEGREES REMARK 500 6 TYR A 225 CB - CG - CD2 ANGL. DEV. = -3.7 DEGREES REMARK 500 15 VAL A 209 CA - CB - CG2 ANGL. DEV. = 9.3 DEGREES REMARK 500 15 TYR A 225 CB - CG - CD1 ANGL. DEV. = -3.6 DEGREES REMARK 500 15 ARG A 228 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES REMARK 500 18 TYR A 225 CB - CG - CD2 ANGL. DEV. = -3.9 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 SER A 132 -65.26 -130.78 REMARK 500 1 ALA A 133 173.98 178.45 REMARK 500 1 VAL A 166 -74.98 -77.04 REMARK 500 1 GLN A 168 74.63 45.21 REMARK 500 1 ASN A 171 -171.86 62.80 REMARK 500 1 SER A 174 37.18 -94.75 REMARK 500 1 ASN A 197 -166.33 50.20 REMARK 500 1 ALA A 226 -113.06 -92.86 REMARK 500 1 GLN A 227 -49.78 -142.55 REMARK 500 1 ALA A 230 -137.34 59.38 REMARK 500 2 ALA A 133 170.04 172.89 REMARK 500 2 GLU A 152 2.26 -67.12 REMARK 500 2 PRO A 165 -171.60 -66.38 REMARK 500 2 ASP A 167 -72.87 -63.16 REMARK 500 2 ASN A 171 -174.05 64.60 REMARK 500 2 SER A 174 39.14 -84.49 REMARK 500 2 PHE A 175 -58.37 -138.53 REMARK 500 2 THR A 183 -70.07 -75.81 REMARK 500 2 HIS A 187 4.62 -62.10 REMARK 500 2 ALA A 226 64.13 13.37 REMARK 500 2 ARG A 228 -47.04 -154.52 REMARK 500 2 ALA A 230 78.15 28.79 REMARK 500 3 VAL A 122 -134.71 45.89 REMARK 500 3 ALA A 133 163.15 147.42 REMARK 500 3 PHE A 141 -26.65 -141.95 REMARK 500 3 PRO A 165 175.95 -53.31 REMARK 500 3 SER A 170 -71.41 -70.50 REMARK 500 3 SER A 174 39.28 -81.69 REMARK 500 3 PHE A 175 -65.05 -137.86 REMARK 500 3 THR A 199 -169.18 -79.55 REMARK 500 3 GLN A 227 -69.58 -137.44 REMARK 500 3 ARG A 228 -35.19 -154.38 REMARK 500 3 ALA A 230 -173.57 49.16 REMARK 500 4 ALA A 133 169.45 173.95 REMARK 500 4 GLU A 152 1.06 -60.30 REMARK 500 4 ASN A 153 22.86 -147.61 REMARK 500 4 PRO A 165 -172.17 -65.58 REMARK 500 4 SER A 170 -73.07 -71.73 REMARK 500 4 SER A 174 37.88 -89.88 REMARK 500 4 PHE A 175 -47.76 -143.98 REMARK 500 4 HIS A 187 1.04 -62.96 REMARK 500 4 TYR A 225 -70.23 -63.95 REMARK 500 4 ALA A 226 93.45 179.16 REMARK 500 4 ALA A 230 -88.81 -69.17 REMARK 500 5 ALA A 133 161.28 170.49 REMARK 500 5 PRO A 165 -165.25 -75.04 REMARK 500 5 SER A 174 38.67 -82.26 REMARK 500 5 PHE A 175 -65.75 -127.35 REMARK 500 5 THR A 183 -62.99 -95.57 REMARK 500 5 ALA A 226 38.65 -89.53 REMARK 500 REMARK 500 THIS ENTRY HAS 201 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS REMARK 500 REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES. REMARK 500 MODEL OMEGA REMARK 500 GLN A 168 TYR A 169 2 -147.02 REMARK 500 GLN A 168 TYR A 169 3 -142.12 REMARK 500 ALA A 230 SER A 231 4 123.89 REMARK 500 GLN A 168 TYR A 169 5 -141.82 REMARK 500 TYR A 169 SER A 170 6 -148.42 REMARK 500 GLN A 168 TYR A 169 8 -149.05 REMARK 500 SER A 135 ARG A 136 9 144.79 REMARK 500 ALA A 230 SER A 231 12 -148.17 REMARK 500 ALA A 230 SER A 231 14 134.94 REMARK 500 ALA A 133 MET A 134 15 138.38 REMARK 500 GLY A 229 ALA A 230 17 144.79 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 1 ARG A 148 0.14 SIDE CHAIN REMARK 500 1 TYR A 155 0.09 SIDE CHAIN REMARK 500 1 ARG A 208 0.09 SIDE CHAIN REMARK 500 1 TYR A 225 0.09 SIDE CHAIN REMARK 500 2 ARG A 148 0.08 SIDE CHAIN REMARK 500 3 ARG A 136 0.08 SIDE CHAIN REMARK 500 3 TYR A 169 0.09 SIDE CHAIN REMARK 500 3 TYR A 218 0.07 SIDE CHAIN REMARK 500 3 TYR A 222 0.10 SIDE CHAIN REMARK 500 5 ARG A 151 0.08 SIDE CHAIN REMARK 500 5 ARG A 156 0.14 SIDE CHAIN REMARK 500 6 TYR A 128 0.07 SIDE CHAIN REMARK 500 6 TYR A 162 0.09 SIDE CHAIN REMARK 500 6 TYR A 163 0.09 SIDE CHAIN REMARK 500 7 ARG A 151 0.08 SIDE CHAIN REMARK 500 7 TYR A 169 0.10 SIDE CHAIN REMARK 500 8 ARG A 164 0.12 SIDE CHAIN REMARK 500 8 TYR A 169 0.08 SIDE CHAIN REMARK 500 9 ARG A 148 0.12 SIDE CHAIN REMARK 500 9 ARG A 151 0.09 SIDE CHAIN REMARK 500 9 TYR A 218 0.07 SIDE CHAIN REMARK 500 9 TYR A 222 0.10 SIDE CHAIN REMARK 500 10 ARG A 148 0.08 SIDE CHAIN REMARK 500 10 TYR A 149 0.09 SIDE CHAIN REMARK 500 11 ARG A 151 0.17 SIDE CHAIN REMARK 500 12 TYR A 149 0.07 SIDE CHAIN REMARK 500 12 TYR A 157 0.07 SIDE CHAIN REMARK 500 13 TYR A 128 0.10 SIDE CHAIN REMARK 500 13 ARG A 136 0.12 SIDE CHAIN REMARK 500 13 TYR A 155 0.11 SIDE CHAIN REMARK 500 13 ARG A 164 0.10 SIDE CHAIN REMARK 500 13 ARG A 228 0.14 SIDE CHAIN REMARK 500 14 ARG A 136 0.12 SIDE CHAIN REMARK 500 14 ARG A 151 0.13 SIDE CHAIN REMARK 500 14 TYR A 155 0.09 SIDE CHAIN REMARK 500 15 ARG A 151 0.13 SIDE CHAIN REMARK 500 15 TYR A 155 0.07 SIDE CHAIN REMARK 500 16 TYR A 155 0.07 SIDE CHAIN REMARK 500 16 ARG A 156 0.10 SIDE CHAIN REMARK 500 18 TYR A 169 0.08 SIDE CHAIN REMARK 500 19 TYR A 222 0.10 SIDE CHAIN REMARK 500 20 ARG A 208 0.10 SIDE CHAIN REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 1XYJ RELATED DB: PDB REMARK 900 CAT PRION PROTEIN REMARK 900 RELATED ID: 1XYK RELATED DB: PDB REMARK 900 DOG PRION PROTEIN REMARK 900 RELATED ID: 6380 RELATED DB: BMRB REMARK 900 CHEMICAL SHIFT OF THE PIG PRION PROTEIN DBREF 1XYQ A 121 231 UNP P49927 PRIO_PIG 125 235 SEQRES 1 A 111 VAL VAL GLY GLY LEU GLY GLY TYR MET LEU GLY SER ALA SEQRES 2 A 111 MET SER ARG PRO LEU ILE HIS PHE GLY SER ASP TYR GLU SEQRES 3 A 111 ASP ARG TYR TYR ARG GLU ASN MET TYR ARG TYR PRO ASN SEQRES 4 A 111 GLN VAL TYR TYR ARG PRO VAL ASP GLN TYR SER ASN GLN SEQRES 5 A 111 ASN SER PHE VAL HIS ASP CYS VAL ASN ILE THR VAL LYS SEQRES 6 A 111 GLN HIS THR VAL THR THR THR THR LYS GLY GLU ASN PHE SEQRES 7 A 111 THR GLU THR ASP VAL LYS MET ILE GLU ARG VAL VAL GLU SEQRES 8 A 111 GLN MET CYS ILE THR GLN TYR GLN LYS GLU TYR GLU ALA SEQRES 9 A 111 TYR ALA GLN ARG GLY ALA SER HELIX 1 1 TYR A 145 TYR A 150 1 6 HELIX 2 2 ARG A 151 TYR A 157 5 7 HELIX 3 3 GLN A 172 THR A 193 1 22 HELIX 4 4 THR A 199 ALA A 226 1 28 SHEET 1 A 2 MET A 129 LEU A 130 0 SHEET 2 A 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 2.04 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