Header list of 1y2s.pdb file
Complete list - r 2 2 Bytes
HEADER UNKNOWN FUNCTION 23-NOV-04 1Y2S TITLE OVINE PRION PROTEIN VARIANT R168 COMPND MOL_ID: 1; COMPND 2 MOLECULE: MAJOR PRION PROTEIN; COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: GLOBULAR DOMAIN, RESIDUES 121-231; COMPND 5 SYNONYM: PRP; COMPND 6 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: OVIS ARIES; SOURCE 3 ORGANISM_COMMON: SHEEP; SOURCE 4 ORGANISM_TAXID: 9940; SOURCE 5 GENE: PRNP; SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 511693; SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21; SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PRSETA KEYWDS PRION PROTEIN, SHEEP, OVPRP, POLYMORPHISM, SCRAPIE, TSE, KEYWDS 2 GLYCOPROTEIN, GPI-ANCHOR, UNKNOWN FUNCTION EXPDTA SOLUTION NMR NUMMDL 20 AUTHOR B.CHRISTEN,D.A.LYSEK,T.HERRMANN,K.WUTHRICH REVDAT 5 02-MAR-22 1Y2S 1 REMARK SEQADV REVDAT 4 24-FEB-09 1Y2S 1 VERSN REVDAT 3 25-JAN-05 1Y2S 1 JRNL REVDAT 2 11-JAN-05 1Y2S 1 AUTHOR REVDAT 1 28-DEC-04 1Y2S 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 : ATNOS, OPALP REMARK 3 AUTHORS : HERRMANN (ATNOS), KORADI, BILLETER, GUENTERT REMARK 3 (OPALP) REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: REMARK 3 THE SEQUENCE NUMBERING GIVEN IN THIS ENTRY IS THAT FOR HUMAN PRION REMARK 3 PROTEIN (RATHER THAN SEQUENTIAL) BASED ON SEQUENCE ALIGNMENT REMARK 4 REMARK 4 1Y2S COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 30-NOV-04. REMARK 100 THE DEPOSITION ID IS D_1000031043. 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 : 0.5-1MM OVPRP-R168, 10MM ACETATE REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY; 3D_13C REMARK 210 -SEPARATED_NOESY REMARK 210 SPECTROMETER FIELD STRENGTH : 900 MHZ; 750 MHZ REMARK 210 SPECTROMETER MODEL : AVANCE; DRX REMARK 210 SPECTROMETER MANUFACTURER : BRUKER REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : CANDID, DYANA 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: 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: COVALENT BOND LENGTHS 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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3) 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 RES CSSEQI ATM2 DEVIATION REMARK 500 10 CYS A 179 CB CYS A 179 SG -0.101 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 1 VAL A 184 CA - CB - CG1 ANGL. DEV. = 10.1 DEGREES REMARK 500 5 ARG A 151 CD - NE - CZ ANGL. DEV. = 8.6 DEGREES REMARK 500 5 VAL A 184 CA - CB - CG1 ANGL. DEV. = 9.7 DEGREES REMARK 500 9 ARG A 156 NE - CZ - NH2 ANGL. DEV. = -3.4 DEGREES REMARK 500 12 CYS A 179 CA - CB - SG ANGL. DEV. = 9.8 DEGREES REMARK 500 14 VAL A 184 CA - CB - CG1 ANGL. DEV. = 9.5 DEGREES REMARK 500 17 VAL A 184 CA - CB - CG1 ANGL. DEV. = 9.5 DEGREES REMARK 500 17 CYS A 214 CA - CB - SG ANGL. DEV. = 8.7 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 VAL A 121 64.80 -151.02 REMARK 500 1 ALA A 133 145.63 78.02 REMARK 500 1 ARG A 136 80.30 23.95 REMARK 500 1 PRO A 137 3.02 -63.58 REMARK 500 1 LEU A 138 103.59 -24.29 REMARK 500 1 GLU A 152 -70.48 -55.72 REMARK 500 1 ASN A 171 173.15 95.17 REMARK 500 1 GLN A 186 0.13 -65.30 REMARK 500 1 GLU A 196 93.46 26.80 REMARK 500 1 PHE A 198 99.31 -64.67 REMARK 500 1 GLU A 221 20.90 -79.62 REMARK 500 1 ALA A 230 -176.56 61.06 REMARK 500 2 ALA A 133 168.16 69.45 REMARK 500 2 ARG A 136 82.02 41.05 REMARK 500 2 PRO A 137 68.39 -68.26 REMARK 500 2 PHE A 141 -73.30 -68.16 REMARK 500 2 VAL A 166 40.65 -80.01 REMARK 500 2 SER A 170 107.91 -160.45 REMARK 500 2 ASN A 171 124.47 54.22 REMARK 500 2 THR A 192 7.42 -68.65 REMARK 500 2 THR A 193 -70.66 -64.09 REMARK 500 2 LYS A 194 10.78 -152.48 REMARK 500 2 GLU A 196 51.17 24.00 REMARK 500 2 ALA A 230 -75.69 -137.70 REMARK 500 3 SER A 120 154.81 72.11 REMARK 500 3 SER A 132 -39.62 -35.84 REMARK 500 3 ALA A 133 139.73 68.95 REMARK 500 3 ARG A 136 81.56 24.90 REMARK 500 3 LEU A 138 91.84 -24.56 REMARK 500 3 GLU A 152 -74.81 -57.42 REMARK 500 3 ASN A 153 31.65 -94.35 REMARK 500 3 ARG A 168 32.87 -168.78 REMARK 500 3 TYR A 169 55.48 37.85 REMARK 500 3 GLU A 196 59.73 -64.86 REMARK 500 3 PHE A 198 -170.94 -62.51 REMARK 500 3 GLU A 221 -134.23 -114.88 REMARK 500 3 SER A 222 -73.68 65.65 REMARK 500 3 ARG A 228 88.20 -156.69 REMARK 500 3 ALA A 230 -76.63 -73.99 REMARK 500 4 SER A 120 64.02 31.30 REMARK 500 4 ALA A 133 148.08 87.72 REMARK 500 4 SER A 135 -179.08 -58.99 REMARK 500 4 LEU A 138 90.14 -24.05 REMARK 500 4 ASP A 167 -103.96 40.50 REMARK 500 4 TYR A 169 7.51 58.24 REMARK 500 4 ASN A 171 -169.66 58.47 REMARK 500 4 GLN A 172 -76.95 -142.45 REMARK 500 4 GLU A 196 101.13 24.08 REMARK 500 5 LEU A 125 -58.06 -134.07 REMARK 500 5 SER A 132 -68.58 53.58 REMARK 500 REMARK 500 THIS ENTRY HAS 241 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 ALA A 230 SER A 231 1 -146.98 REMARK 500 GLY A 119 SER A 120 5 143.08 REMARK 500 SER A 132 ALA A 133 7 -149.93 REMARK 500 GLY A 195 GLU A 196 9 145.59 REMARK 500 TYR A 163 ARG A 164 19 149.55 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 TYR A 128 0.12 SIDE CHAIN REMARK 500 1 TYR A 155 0.07 SIDE CHAIN REMARK 500 1 TYR A 157 0.07 SIDE CHAIN REMARK 500 2 TYR A 149 0.10 SIDE CHAIN REMARK 500 3 TYR A 155 0.07 SIDE CHAIN REMARK 500 3 TYR A 157 0.07 SIDE CHAIN REMARK 500 4 TYR A 128 0.08 SIDE CHAIN REMARK 500 4 ARG A 156 0.16 SIDE CHAIN REMARK 500 4 TYR A 225 0.11 SIDE CHAIN REMARK 500 5 TYR A 157 0.07 SIDE CHAIN REMARK 500 5 ARG A 208 0.08 SIDE CHAIN REMARK 500 5 TYR A 225 0.09 SIDE CHAIN REMARK 500 6 TYR A 155 0.09 SIDE CHAIN REMARK 500 6 TYR A 162 0.08 SIDE CHAIN REMARK 500 7 TYR A 169 0.10 SIDE CHAIN REMARK 500 7 ARG A 220 0.09 SIDE CHAIN REMARK 500 8 ARG A 151 0.15 SIDE CHAIN REMARK 500 8 TYR A 155 0.08 SIDE CHAIN REMARK 500 8 TYR A 162 0.07 SIDE CHAIN REMARK 500 8 ARG A 164 0.08 SIDE CHAIN REMARK 500 8 ARG A 168 0.09 SIDE CHAIN REMARK 500 8 ARG A 208 0.08 SIDE CHAIN REMARK 500 9 ARG A 168 0.08 SIDE CHAIN REMARK 500 10 TYR A 128 0.07 SIDE CHAIN REMARK 500 10 ARG A 156 0.09 SIDE CHAIN REMARK 500 10 TYR A 225 0.08 SIDE CHAIN REMARK 500 11 TYR A 155 0.11 SIDE CHAIN REMARK 500 11 ARG A 168 0.09 SIDE CHAIN REMARK 500 11 TYR A 225 0.08 SIDE CHAIN REMARK 500 12 ARG A 156 0.14 SIDE CHAIN REMARK 500 13 TYR A 162 0.09 SIDE CHAIN REMARK 500 13 TYR A 163 0.11 SIDE CHAIN REMARK 500 13 ARG A 208 0.10 SIDE CHAIN REMARK 500 14 ARG A 148 0.15 SIDE CHAIN REMARK 500 14 TYR A 155 0.11 SIDE CHAIN REMARK 500 14 TYR A 162 0.11 SIDE CHAIN REMARK 500 14 ARG A 168 0.08 SIDE CHAIN REMARK 500 14 TYR A 218 0.10 SIDE CHAIN REMARK 500 15 TYR A 226 0.07 SIDE CHAIN REMARK 500 16 TYR A 157 0.09 SIDE CHAIN REMARK 500 16 TYR A 162 0.10 SIDE CHAIN REMARK 500 16 TYR A 169 0.08 SIDE CHAIN REMARK 500 16 TYR A 218 0.07 SIDE CHAIN REMARK 500 17 TYR A 128 0.11 SIDE CHAIN REMARK 500 17 TYR A 162 0.08 SIDE CHAIN REMARK 500 17 TYR A 225 0.08 SIDE CHAIN REMARK 500 18 ARG A 136 0.08 SIDE CHAIN REMARK 500 18 ARG A 148 0.11 SIDE CHAIN REMARK 500 18 ARG A 208 0.09 SIDE CHAIN REMARK 500 18 TYR A 226 0.07 SIDE CHAIN REMARK 500 REMARK 500 THIS ENTRY HAS 59 PLANE DEVIATIONS. REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 1XYU RELATED DB: PDB REMARK 900 OVINE PRION PROTEIN VARIANT H168 DBREF 1Y2S A 121 231 UNP P23907 PRIO_SHEEP 124 234 SEQADV 1Y2S GLY A 119 UNP P23907 CLONING ARTIFACT SEQADV 1Y2S SER A 120 UNP P23907 CLONING ARTIFACT SEQRES 1 A 113 GLY SER VAL VAL GLY GLY LEU GLY GLY TYR MET LEU GLY SEQRES 2 A 113 SER ALA MET SER ARG PRO LEU ILE HIS PHE GLY ASN ASP SEQRES 3 A 113 TYR GLU ASP ARG TYR TYR ARG GLU ASN MET TYR ARG TYR SEQRES 4 A 113 PRO ASN GLN VAL TYR TYR ARG PRO VAL ASP ARG TYR SER SEQRES 5 A 113 ASN GLN ASN ASN PHE VAL HIS ASP CYS VAL ASN ILE THR SEQRES 6 A 113 VAL LYS GLN HIS THR VAL THR THR THR THR LYS GLY GLU SEQRES 7 A 113 ASN PHE THR GLU THR ASP ILE LYS ILE MET GLU ARG VAL SEQRES 8 A 113 VAL GLU GLN MET CYS ILE THR GLN TYR GLN ARG GLU SER SEQRES 9 A 113 GLN ALA TYR TYR GLN ARG GLY ALA SER HELIX 1 1 GLY A 124 TYR A 128 5 5 HELIX 2 2 ASP A 144 MET A 154 1 11 HELIX 3 3 GLN A 172 THR A 193 1 22 HELIX 4 4 THR A 199 GLN A 219 1 21 HELIX 5 5 GLU A 221 ARG A 228 1 8 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 2.32 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