Header list of 1dx1.pdb file
Complete list - g 5 2 Bytes
HEADER PROTEIN FIBRIL 15-DEC-99 1DX1 TITLE BOVINE PRION PROTEIN RESIDUES 23-230 COMPND MOL_ID: 1; COMPND 2 MOLECULE: PRION PROTEIN; COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: RESIDUES 23-230; COMPND 5 SYNONYM: PRP, MAJOR PRION PROTEIN; COMPND 6 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: BOS TAURUS; SOURCE 3 ORGANISM_COMMON: BOVINE; SOURCE 4 ORGANISM_TAXID: 9913; SOURCE 5 ORGAN: BRAIN; SOURCE 6 CELLULAR_LOCATION: EXTRACELLULAR; SOURCE 7 GENE: PRNP; SOURCE 8 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 9 EXPRESSION_SYSTEM_TAXID: 469008; SOURCE 10 EXPRESSION_SYSTEM_STRAIN: BL21(DE3); SOURCE 11 EXPRESSION_SYSTEM_CELLULAR_LOCATION: CYTOPLASM; SOURCE 12 EXPRESSION_SYSTEM_PLASMID: PRSET A KEYWDS PROTEIN FIBRIL, PRION PROTEIN, REPEAT STRUCTURE EXPDTA SOLUTION NMR NUMMDL 20 AUTHOR F.LOPEZ-GARCIA,R.ZAHN,R.RIEK,M.BILLETER,K.WUTHRICH REVDAT 7 05-AUG-15 1DX1 1 REMARK DBREF SEQADV REVDAT 6 21-MAR-12 1DX1 1 HEADER COMPND KEYWDS REMARK REVDAT 6 2 VERSN HETNAM SSBOND ATOM REVDAT 6 3 TER REVDAT 5 24-FEB-09 1DX1 1 VERSN REVDAT 4 04-APR-05 1DX1 1 ATOM REVDAT 3 27-FEB-04 1DX1 1 SSBOND ATOM CONECT REVDAT 2 26-FEB-02 1DX1 1 TITLE JRNL REMARK REVDAT 1 20-JUL-00 1DX1 0 JRNL AUTH F.LOPEZ-GARCIA,R.ZAHN,R.RIEK,K.WUTHRICH JRNL TITL NMR STRUCTURE OF THE BOVINE PRION PROTEIN JRNL REF PROC.NATL.ACAD.SCI.USA V. 97 8334 2000 JRNL REFN ISSN 0027-8424 JRNL PMID 10899999 JRNL DOI 10.1073/PNAS.97.15.8334 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : OPALP REMARK 3 AUTHORS : KORADI, BILLETER,GUNTERT REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 1DX1 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 16-DEC-99. REMARK 100 THE PDBE ID CODE IS EBI-4474. 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 : 0.01 REMARK 210 PRESSURE : 1 ATM REMARK 210 SAMPLE CONTENTS : 90% WATER/10% D2O REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : NOESY; COSY REMARK 210 SPECTROMETER FIELD STRENGTH : 750 REMARK 210 SPECTROMETER MODEL : DRX750 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 : 50 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20 REMARK 210 CONFORMERS, SELECTION CRITERIA : LEAST RESTRAINT VIOLATION REMARK 210 REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 3 REMARK 210 REMARK 210 REMARK: CLOSEST TO THE MEAN REMARK 210 (BACKBONE HEAVY ATOMS OF RESIDUES 125-227). THE STRUCTURE REMARK 210 WAS DETERMINED USING TRIPLE-RESONANCE NMR SPECTROSCOPY ON REMARK 210 13C, 15N-LABELED PROTEIN 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 400 REMARK 400 COMPOUND REMARK 400 THE PDB ENTRIES 1DWY, 1DWZ, 1DX0 AND 1DX1 FORM REMARK 400 A SET OF STRUCTURE DETERMINATIONS AS: REMARK 400 1DWY THE MINIMIZED CONFORMER CLOSEST TO THE MEAN REMARK 400 OF THE FRAGMENT BPRP(121-230) (ONLY SUBMITTED REMARK 400 RESIDUES 124-227) REMARK 400 1DWZ 20 MINIMIZED CONFORMERS OF THE FRAGMENT BPRP(121-230) REMARK 400 (ONLY SUBMITTED RESIDUES 124-227) REMARK 400 1DX0 THE MINIMIZED CONFORMER CLOSEST TO THE MEAN OF REMARK 400 THE FULL LENGTH BPRP(23-230) (ONLY SUBMITTED RESIDUES REMARK 400 124-227) REMARK 400 1DX1 20 MINIMIZED CONFORMERS OF THE FULL LENGTH BPRP(23-230) REMARK 400 (ONLY SUBMITTED RESIDUES 124-227) REMARK 400 REMARK 400 THE SEQUENCE NUMBERING GIVEN IN THESE ENTRIES IS THAT REMARK 400 FOR HUMAN PRION PROTEIN (RATHER THAN SEQUENTIAL) BASED REMARK 400 ON SEQUENCE ALIGNMENT. REMARK 465 REMARK 465 MISSING RESIDUES REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.) REMARK 465 MODELS 1- 20 REMARK 465 RES C SSSEQI REMARK 465 GLY A 12 REMARK 465 SER A 13 REMARK 465 LYS A 14 REMARK 465 LYS A 15 REMARK 465 ARG A 16 REMARK 465 PRO A 17 REMARK 465 LYS A 18 REMARK 465 PRO A 19 REMARK 465 GLY A 20 REMARK 465 GLY A 21 REMARK 465 GLY A 22 REMARK 465 TRP A 23 REMARK 465 ASN A 24 REMARK 465 THR A 25 REMARK 465 GLY A 26 REMARK 465 GLY A 27 REMARK 465 SER A 28 REMARK 465 ARG A 29 REMARK 465 TYR A 30 REMARK 465 PRO A 31 REMARK 465 GLY A 32 REMARK 465 GLN A 33 REMARK 465 GLY A 34 REMARK 465 SER A 35 REMARK 465 PRO A 36 REMARK 465 GLY A 37 REMARK 465 GLY A 38 REMARK 465 ASN A 39 REMARK 465 ARG A 40 REMARK 465 TYR A 41 REMARK 465 PRO A 42 REMARK 465 PRO A 43 REMARK 465 GLN A 44 REMARK 465 GLY A 45 REMARK 465 GLY A 46 REMARK 465 GLY A 47 REMARK 465 GLY A 48 REMARK 465 TRP A 49 REMARK 465 GLY A 50 REMARK 465 GLN A 51 REMARK 465 PRO A 52 REMARK 465 HIS A 53 REMARK 465 GLY A 54 REMARK 465 GLY A 55 REMARK 465 GLY A 56 REMARK 465 TRP A 57 REMARK 465 GLY A 58 REMARK 465 GLN A 59 REMARK 465 PRO A 60 REMARK 465 HIS A 61 REMARK 465 GLY A 62 REMARK 465 GLY A 63 REMARK 465 GLY A 64 REMARK 465 TRP A 65 REMARK 465 GLY A 66 REMARK 465 GLN A 67 REMARK 465 PRO A 68 REMARK 465 HIS A 69 REMARK 465 GLY A 70 REMARK 465 GLY A 71 REMARK 465 GLY A 72 REMARK 465 TRP A 73 REMARK 465 GLY A 74 REMARK 465 GLN A 75 REMARK 465 PRO A 76 REMARK 465 HIS A 77 REMARK 465 GLY A 78 REMARK 465 GLY A 79 REMARK 465 GLY A 80 REMARK 465 TRP A 81 REMARK 465 GLY A 82 REMARK 465 GLN A 83 REMARK 465 PRO A 84 REMARK 465 HIS A 85 REMARK 465 GLY A 86 REMARK 465 GLY A 87 REMARK 465 GLY A 88 REMARK 465 GLY A 89 REMARK 465 TRP A 90 REMARK 465 GLY A 91 REMARK 465 GLN A 92 REMARK 465 GLY A 93 REMARK 465 GLY A 94 REMARK 465 THR A 95 REMARK 465 HIS A 96 REMARK 465 GLY A 97 REMARK 465 GLN A 98 REMARK 465 TRP A 99 REMARK 465 ASN A 100 REMARK 465 LYS A 101 REMARK 465 PRO A 102 REMARK 465 SER A 103 REMARK 465 LYS A 104 REMARK 465 PRO A 105 REMARK 465 LYS A 106 REMARK 465 THR A 107 REMARK 465 ASN A 108 REMARK 465 MET A 109 REMARK 465 LYS A 110 REMARK 465 HIS A 111 REMARK 465 VAL A 112 REMARK 465 ALA A 113 REMARK 465 GLY A 114 REMARK 465 ALA A 115 REMARK 465 ALA A 116 REMARK 465 ALA A 117 REMARK 465 ALA A 118 REMARK 465 GLY A 119 REMARK 465 ALA A 120 REMARK 465 VAL A 121 REMARK 465 VAL A 122 REMARK 465 GLY A 123 REMARK 465 ARG A 228 REMARK 465 GLY A 229 REMARK 465 ALA A 230 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 HH TYR A 157 OD1 ASP A 202 1.59 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 2 ARG A 156 NE - CZ - NH2 ANGL. DEV. = -3.0 DEGREES REMARK 500 2 TYR A 162 CB - CG - CD2 ANGL. DEV. = -4.1 DEGREES REMARK 500 2 VAL A 209 CA - CB - CG1 ANGL. DEV. = 9.1 DEGREES REMARK 500 3 TYR A 128 CB - CG - CD1 ANGL. DEV. = -4.3 DEGREES REMARK 500 3 ARG A 156 CD - NE - CZ ANGL. DEV. = 9.5 DEGREES REMARK 500 4 TYR A 163 CB - CG - CD2 ANGL. DEV. = -3.6 DEGREES REMARK 500 4 VAL A 209 CA - CB - CG1 ANGL. DEV. = 10.0 DEGREES REMARK 500 5 TYR A 163 CB - CG - CD2 ANGL. DEV. = -3.7 DEGREES REMARK 500 7 ARG A 220 NE - CZ - NH2 ANGL. DEV. = -3.1 DEGREES REMARK 500 8 ARG A 164 NE - CZ - NH2 ANGL. DEV. = -3.2 DEGREES REMARK 500 8 VAL A 209 CA - CB - CG2 ANGL. DEV. = 12.3 DEGREES REMARK 500 9 VAL A 176 CA - CB - CG2 ANGL. DEV. = 11.7 DEGREES REMARK 500 13 TYR A 162 CB - CG - CD2 ANGL. DEV. = -3.7 DEGREES REMARK 500 16 VAL A 176 CA - CB - CG2 ANGL. DEV. = 9.9 DEGREES REMARK 500 16 CYS A 179 CA - CB - SG ANGL. DEV. = 6.6 DEGREES REMARK 500 17 PHE A 175 CB - CG - CD1 ANGL. DEV. = -4.4 DEGREES REMARK 500 17 VAL A 209 CA - CB - CG1 ANGL. DEV. = 9.2 DEGREES REMARK 500 20 THR A 191 CA - CB - OG1 ANGL. DEV. = 13.9 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 LEU A 125 -70.55 -84.80 REMARK 500 1 TYR A 150 2.10 -67.53 REMARK 500 1 TYR A 163 -154.08 -157.55 REMARK 500 1 ASP A 167 -94.13 35.18 REMARK 500 1 SER A 170 93.45 -60.79 REMARK 500 1 GLN A 172 -87.43 -98.12 REMARK 500 2 TYR A 128 -161.75 51.55 REMARK 500 2 PHE A 141 -63.68 -137.31 REMARK 500 2 PRO A 165 162.72 -49.91 REMARK 500 2 SER A 170 100.01 -34.27 REMARK 500 2 GLN A 172 -67.83 -121.61 REMARK 500 3 TYR A 128 -159.55 42.22 REMARK 500 3 GLN A 168 133.84 95.57 REMARK 500 3 GLN A 172 -75.58 -91.76 REMARK 500 4 LEU A 125 -99.43 -80.54 REMARK 500 4 HIS A 140 49.05 -78.31 REMARK 500 4 ASP A 167 -68.69 63.59 REMARK 500 4 TYR A 169 15.14 56.43 REMARK 500 4 GLU A 186 44.73 -77.67 REMARK 500 4 HIS A 187 -76.69 -140.97 REMARK 500 5 MET A 154 -61.09 -24.82 REMARK 500 5 ASN A 159 16.46 -143.64 REMARK 500 5 PRO A 165 -175.92 -68.46 REMARK 500 5 VAL A 166 -83.44 -65.28 REMARK 500 5 ASP A 167 -150.52 55.66 REMARK 500 5 GLN A 168 -179.52 -59.36 REMARK 500 5 TYR A 169 80.17 60.00 REMARK 500 5 SER A 170 -165.60 -72.24 REMARK 500 5 ASN A 171 104.56 93.62 REMARK 500 5 TYR A 226 69.51 -117.77 REMARK 500 6 TYR A 128 -174.36 49.41 REMARK 500 6 SER A 132 177.47 62.39 REMARK 500 6 PHE A 141 -84.58 -70.11 REMARK 500 6 ASN A 153 20.56 -78.88 REMARK 500 7 SER A 132 -177.76 57.09 REMARK 500 7 ASP A 167 -152.13 -76.14 REMARK 500 7 GLN A 168 -85.02 55.13 REMARK 500 7 GLU A 186 25.41 -72.70 REMARK 500 7 HIS A 187 -65.46 -125.64 REMARK 500 8 TYR A 128 -156.86 48.07 REMARK 500 8 HIS A 140 71.92 -103.43 REMARK 500 8 ASP A 167 48.38 -73.26 REMARK 500 8 GLN A 168 -35.96 -153.08 REMARK 500 8 SER A 170 70.09 47.39 REMARK 500 9 ASP A 167 -89.03 34.74 REMARK 500 9 TYR A 169 91.92 69.33 REMARK 500 9 SER A 170 77.09 -151.39 REMARK 500 10 SER A 132 174.39 63.52 REMARK 500 10 PHE A 141 -70.18 -130.01 REMARK 500 10 GLN A 168 -176.64 61.39 REMARK 500 REMARK 500 THIS ENTRY HAS 122 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 ASN A 171 GLN A 172 2 141.36 REMARK 500 MET A 134 SER A 135 15 148.46 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 218 0.07 SIDE CHAIN REMARK 500 2 ARG A 156 0.10 SIDE CHAIN REMARK 500 2 ARG A 208 0.08 SIDE CHAIN REMARK 500 3 TYR A 128 0.10 SIDE CHAIN REMARK 500 3 TYR A 149 0.09 SIDE CHAIN REMARK 500 3 TYR A 157 0.10 SIDE CHAIN REMARK 500 3 TYR A 162 0.07 SIDE CHAIN REMARK 500 3 TYR A 225 0.09 SIDE CHAIN REMARK 500 4 TYR A 128 0.08 SIDE CHAIN REMARK 500 4 TYR A 150 0.11 SIDE CHAIN REMARK 500 4 ARG A 164 0.08 SIDE CHAIN REMARK 500 5 ARG A 136 0.08 SIDE CHAIN REMARK 500 5 TYR A 149 0.10 SIDE CHAIN REMARK 500 5 TYR A 150 0.07 SIDE CHAIN REMARK 500 5 TYR A 162 0.11 SIDE CHAIN REMARK 500 5 ARG A 164 0.08 SIDE CHAIN REMARK 500 6 TYR A 145 0.06 SIDE CHAIN REMARK 500 6 TYR A 150 0.07 SIDE CHAIN REMARK 500 6 ARG A 156 0.12 SIDE CHAIN REMARK 500 6 TYR A 157 0.10 SIDE CHAIN REMARK 500 7 ARG A 208 0.08 SIDE CHAIN REMARK 500 7 ARG A 220 0.14 SIDE CHAIN REMARK 500 8 TYR A 149 0.09 SIDE CHAIN REMARK 500 8 TYR A 150 0.09 SIDE CHAIN REMARK 500 9 TYR A 225 0.07 SIDE CHAIN REMARK 500 10 TYR A 128 0.08 SIDE CHAIN REMARK 500 10 ARG A 136 0.08 SIDE CHAIN REMARK 500 10 TYR A 150 0.13 SIDE CHAIN REMARK 500 10 ARG A 156 0.08 SIDE CHAIN REMARK 500 10 TYR A 218 0.08 SIDE CHAIN REMARK 500 11 TYR A 145 0.08 SIDE CHAIN REMARK 500 11 ARG A 148 0.10 SIDE CHAIN REMARK 500 11 ARG A 156 0.09 SIDE CHAIN REMARK 500 11 TYR A 218 0.08 SIDE CHAIN REMARK 500 12 ARG A 136 0.08 SIDE CHAIN REMARK 500 12 TYR A 150 0.14 SIDE CHAIN REMARK 500 12 ARG A 151 0.08 SIDE CHAIN REMARK 500 12 TYR A 163 0.11 SIDE CHAIN REMARK 500 12 ARG A 208 0.10 SIDE CHAIN REMARK 500 13 ARG A 151 0.12 SIDE CHAIN REMARK 500 13 TYR A 157 0.08 SIDE CHAIN REMARK 500 13 ARG A 220 0.13 SIDE CHAIN REMARK 500 14 TYR A 145 0.12 SIDE CHAIN REMARK 500 14 TYR A 150 0.07 SIDE CHAIN REMARK 500 14 TYR A 163 0.07 SIDE CHAIN REMARK 500 14 TYR A 218 0.11 SIDE CHAIN REMARK 500 15 TYR A 128 0.08 SIDE CHAIN REMARK 500 15 ARG A 136 0.08 SIDE CHAIN REMARK 500 15 TYR A 145 0.11 SIDE CHAIN REMARK 500 15 TYR A 149 0.07 SIDE CHAIN REMARK 500 REMARK 500 THIS ENTRY HAS 61 PLANE DEVIATIONS. REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 1DWZ RELATED DB: PDB REMARK 900 BOVINE PRION PROTEIN FRAGMENT 121-230 NMR, 20 STRUCTURES REMARK 900 RELATED ID: 1DWY RELATED DB: PDB REMARK 900 BOVINE PRION PROTEIN FRAGMENT 121-230 NMR,REPRESENTATIVE REMARK 900 MINIMIZED STRUCTURE REMARK 900 RELATED ID: 1DX0 RELATED DB: PDB REMARK 900 BOVINE PRION PROTEIN NMR, REPRESENTATIVE MINIMIZED STRUCTURE REMARK 900 RELATED ID: 1AG2 RELATED DB: PDB REMARK 900 PRION PROTEIN DOMAIN PRP(121-231) FROM MOUSE, NMR, REMARK 900 MINIMIZED AVERAGE STRUCTURE REMARK 900 RELATED ID: 1B10 RELATED DB: PDB REMARK 900 SOLUTION NMR STRUCTURE OF RECOMBINANT SYRIAN HAMSTER PRION REMARK 900 PROTEIN RPRP(90-231), 25 STRUCTURES REMARK 900 RELATED ID: 1QLX RELATED DB: PDB REMARK 900 HUMAN PRION PROTEIN RESIDUES 23-230 NMR, REMARK 900 REPRESENTATIVE STRUCTURE REMARK 900 RELATED ID: 1QM0 RELATED DB: PDB REMARK 900 HUMAN PRION PROTEIN FRAGMENT 90-230 NMR, REMARK 900 REPRESENTATIVE STRUCTURE REMARK 900 RELATED ID: 1QM1 RELATED DB: PDB REMARK 900 HUMAN PRION PROTEIN FRAGMENT 90-230 NMR, 20 STRUCTURES REMARK 900 RELATED ID: 1QM2 RELATED DB: PDB REMARK 900 HUMAN PRION PROTEIN FRAGMENT 121-230 NMR, REMARK 900 REPRESENTATIVE STRUCTURE REMARK 900 RELATED ID: 1QM3 RELATED DB: PDB REMARK 900 HUMAN PRION PROTEIN FRAGMENT 121-230 NMR, 20 STRUCTURES REMARK 999 REMARK 999 SEQUENCE REMARK 999 RESIDUES (GLY SER) INSERTED AT THE N-TERMINUS REMARK 999 GLY A 21 CLONING ARTIFACT REMARK 999 SER A 22 CLONING ARTIFACT DBREF 1DX1 A 14 230 UNP P10279 PRIO_BOVIN 25 241 SEQADV 1DX1 GLY A 12 UNP P10279 CLONING ARTIFACT SEQADV 1DX1 SER A 13 UNP P10279 CLONING ARTIFACT SEQRES 1 A 219 GLY SER LYS LYS ARG PRO LYS PRO GLY GLY GLY TRP ASN SEQRES 2 A 219 THR GLY GLY SER ARG TYR PRO GLY GLN GLY SER PRO GLY SEQRES 3 A 219 GLY ASN ARG TYR PRO PRO GLN GLY GLY GLY GLY TRP GLY SEQRES 4 A 219 GLN PRO HIS GLY GLY GLY TRP GLY GLN PRO HIS GLY GLY SEQRES 5 A 219 GLY TRP GLY GLN PRO HIS GLY GLY GLY TRP GLY GLN PRO SEQRES 6 A 219 HIS GLY GLY GLY TRP GLY GLN PRO HIS GLY GLY GLY GLY SEQRES 7 A 219 TRP GLY GLN GLY GLY THR HIS GLY GLN TRP ASN LYS PRO SEQRES 8 A 219 SER LYS PRO LYS THR ASN MET LYS HIS VAL ALA GLY ALA SEQRES 9 A 219 ALA ALA ALA GLY ALA VAL VAL GLY GLY LEU GLY GLY TYR SEQRES 10 A 219 MET LEU GLY SER ALA MET SER ARG PRO LEU ILE HIS PHE SEQRES 11 A 219 GLY SER ASP TYR GLU ASP ARG TYR TYR ARG GLU ASN MET SEQRES 12 A 219 HIS ARG TYR PRO ASN GLN VAL TYR TYR ARG PRO VAL ASP SEQRES 13 A 219 GLN TYR SER ASN GLN ASN ASN PHE VAL HIS ASP CYS VAL SEQRES 14 A 219 ASN ILE THR VAL LYS GLU HIS THR VAL THR THR THR THR SEQRES 15 A 219 LYS GLY GLU ASN PHE THR GLU THR ASP ILE LYS MET MET SEQRES 16 A 219 GLU ARG VAL VAL GLU GLN MET CYS ILE THR GLN TYR GLN SEQRES 17 A 219 ARG GLU SER GLN ALA TYR TYR GLN ARG GLY ALA HELIX 1 H1 ASP A 144 GLU A 152 1 9 HELIX 2 H2 ASN A 173 THR A 192 1 20 HELIX 3 H3 GLU A 200 TYR A 225 1 26 SHEET 1 A 2 TYR A 128 GLY A 131 0 SHEET 2 A 2 VAL A 161 ARG A 164 -1 O TYR A 163 N MET A 129 SSBOND 1 CYS A 179 CYS A 214 1555 1555 2.01 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 - g 5 2 Bytes