Header list of 1e1p.pdb file
Complete list - r 25 2 Bytes
HEADER PRION PROTEIN 09-MAY-00 1E1P
TITLE HUMAN PRION PROTEIN VARIANT S170N
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PRION PROTEIN;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: GLOBULAR DOMAIN RESIDUES 125-228;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: 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
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR L.CALZOLAI,D.A.LYSEK,P.GUNTERT,C.VON SCHROETTER,R.ZAHN,
AUTHOR 2 R.RIEK,K.WUTHRICH
REVDAT 2 24-FEB-09 1E1P 1 VERSN
REVDAT 1 20-JUL-00 1E1P 0
JRNL AUTH L.CALZOLAI,D.A.LYSEK,P.GUNTERT,C.VON SCHROETTER,
JRNL AUTH 2 R.ZAHN,R.RIEK,K.WUTHRICH
JRNL TITL NMR STRUCTURES OF THREE SINGLE-RESIDUE VARIANTS OF
JRNL TITL 2 THE HUMAN PRION PROTEIN
JRNL REF PROC.NATL.ACAD.SCI.USA V. 97 8340 2000
JRNL REFN ISSN 0027-8424
JRNL PMID 10900000
JRNL DOI 10.1073/PNAS.97.15.8340
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 1E1P COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 10-MAY-00.
REMARK 100 THE PDBE ID CODE IS EBI-4925.
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 : 50 MM SODIUM ACETATE
REMARK 210 PRESSURE : NULL
REMARK 210 SAMPLE CONTENTS : NULL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : NULL
REMARK 210 SPECTROMETER FIELD STRENGTH : 750
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 : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : NULL
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 9
REMARK 210
REMARK 210 REMARK: 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 400
REMARK 400 COMPOUND
REMARK 400 CHAIN A ENGINEERED MUATATION SER170ASN
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 CYS A 179 CA - CB - SG ANGL. DEV. = 7.0 DEGREES
REMARK 500 11 CYS A 214 CA - CB - SG ANGL. DEV. = -9.4 DEGREES
REMARK 500 11 TYR A 218 CB - CG - CD2 ANGL. DEV. = -3.7 DEGREES
REMARK 500 12 TYR A 226 CB - CG - CD1 ANGL. DEV. = -6.6 DEGREES
REMARK 500 14 CYS A 214 CA - CB - SG ANGL. DEV. = 7.5 DEGREES
REMARK 500 14 ARG A 220 NE - CZ - NH2 ANGL. DEV. = -3.2 DEGREES
REMARK 500 17 TYR A 157 CB - CG - CD2 ANGL. DEV. = -4.2 DEGREES
REMARK 500 17 CYS A 179 CA - CB - SG ANGL. DEV. = 6.8 DEGREES
REMARK 500 19 ARG A 220 NE - CZ - NH2 ANGL. DEV. = -3.4 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 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 135 -166.85 -71.06
REMARK 500 1 MET A 154 -86.84 -58.43
REMARK 500 1 HIS A 155 -85.50 34.35
REMARK 500 1 MET A 166 -82.65 -43.47
REMARK 500 1 GLU A 168 -23.38 95.47
REMARK 500 1 ASN A 170 120.91 -34.69
REMARK 500 2 MET A 134 -164.10 -126.71
REMARK 500 2 MET A 154 -75.70 -33.66
REMARK 500 2 HIS A 155 -71.13 34.76
REMARK 500 2 MET A 166 100.87 -41.40
REMARK 500 2 GLU A 168 -16.02 69.95
REMARK 500 3 SER A 135 173.66 -59.93
REMARK 500 3 MET A 154 -73.33 -41.03
REMARK 500 3 HIS A 155 -73.68 36.66
REMARK 500 3 TYR A 163 -178.39 -175.46
REMARK 500 3 GLU A 168 -32.70 -163.22
REMARK 500 3 ASN A 170 71.05 35.54
REMARK 500 3 GLN A 172 -73.04 -121.25
REMARK 500 4 MET A 154 -79.38 -38.22
REMARK 500 4 HIS A 155 -87.76 33.03
REMARK 500 4 GLU A 168 -27.07 70.58
REMARK 500 4 ASN A 197 24.82 -78.46
REMARK 500 5 SER A 135 -153.29 -79.22
REMARK 500 5 MET A 154 -82.33 -24.69
REMARK 500 5 HIS A 155 -70.10 33.46
REMARK 500 5 PRO A 158 -176.96 -61.76
REMARK 500 5 ASN A 159 -33.11 -138.15
REMARK 500 5 MET A 166 -67.25 -29.36
REMARK 500 5 ASP A 167 30.75 38.22
REMARK 500 5 TYR A 169 -38.38 -142.08
REMARK 500 5 GLN A 172 -73.98 -67.36
REMARK 500 5 GLU A 196 134.24 -30.62
REMARK 500 6 SER A 135 -166.68 -68.82
REMARK 500 6 MET A 154 -81.56 -37.21
REMARK 500 6 HIS A 155 -94.06 34.78
REMARK 500 6 ASP A 167 -37.96 166.76
REMARK 500 6 GLU A 168 -35.94 -149.71
REMARK 500 6 ASN A 170 -161.28 52.35
REMARK 500 6 ASN A 171 -162.82 49.92
REMARK 500 7 SER A 135 -163.35 -74.91
REMARK 500 7 PRO A 137 -171.69 -69.66
REMARK 500 7 MET A 154 -80.23 -24.64
REMARK 500 7 HIS A 155 -84.34 33.56
REMARK 500 7 MET A 166 99.23 -62.10
REMARK 500 7 ASP A 167 46.09 -81.53
REMARK 500 7 GLU A 168 -4.54 63.53
REMARK 500 7 ASN A 171 -68.71 -141.25
REMARK 500 7 GLN A 172 -75.94 -120.20
REMARK 500 7 THR A 192 6.72 -67.72
REMARK 500 8 SER A 135 -161.29 -72.04
REMARK 500 8 MET A 154 -76.67 -36.58
REMARK 500 8 HIS A 155 -74.84 33.66
REMARK 500 8 PRO A 158 174.06 -55.83
REMARK 500 8 ASP A 167 -32.36 151.39
REMARK 500 8 GLU A 168 -45.40 -156.79
REMARK 500 8 ASN A 170 174.31 52.09
REMARK 500 8 ASN A 171 143.83 85.23
REMARK 500 8 PHE A 175 6.41 -65.73
REMARK 500 8 PHE A 198 75.24 24.86
REMARK 500 9 MET A 134 -175.81 -69.87
REMARK 500 9 SER A 135 -153.08 -70.62
REMARK 500 9 MET A 154 -74.82 -29.07
REMARK 500 9 HIS A 155 -78.14 35.54
REMARK 500 9 ASN A 159 -48.82 -146.76
REMARK 500 9 ASP A 167 -50.60 171.07
REMARK 500 9 GLU A 168 -35.36 167.75
REMARK 500 9 ASN A 171 -166.17 -161.99
REMARK 500 9 GLN A 172 -75.93 -74.37
REMARK 500 10 MET A 154 -101.44 -62.50
REMARK 500 10 HIS A 155 -88.48 35.42
REMARK 500 10 ASN A 159 -42.83 -131.32
REMARK 500 10 MET A 166 154.68 -48.24
REMARK 500 10 ASP A 167 -48.35 174.62
REMARK 500 10 GLU A 168 -46.61 -151.21
REMARK 500 10 ASN A 170 78.33 33.83
REMARK 500 10 GLN A 172 -75.35 -99.13
REMARK 500 10 THR A 199 172.65 -57.14
REMARK 500 11 SER A 135 173.94 -57.57
REMARK 500 11 MET A 154 -76.85 -29.77
REMARK 500 11 HIS A 155 -93.79 32.97
REMARK 500 11 PHE A 198 94.72 -64.25
REMARK 500 12 SER A 135 -167.00 -66.46
REMARK 500 12 MET A 154 -71.22 -31.48
REMARK 500 12 HIS A 155 -93.48 32.99
REMARK 500 12 PRO A 165 -170.09 -68.23
REMARK 500 12 MET A 166 82.25 -45.48
REMARK 500 12 GLU A 168 -40.85 81.27
REMARK 500 12 ASN A 171 -147.87 49.38
REMARK 500 12 GLN A 172 -71.81 -113.60
REMARK 500 13 SER A 135 -169.96 -64.80
REMARK 500 13 MET A 154 -92.79 -35.06
REMARK 500 13 HIS A 155 -82.75 32.63
REMARK 500 13 GLU A 168 -33.15 -164.73
REMARK 500 13 TYR A 169 -34.49 -24.33
REMARK 500 13 ASN A 170 109.33 34.44
REMARK 500 13 GLN A 172 -75.14 -95.00
REMARK 500 13 THR A 192 -5.73 -59.65
REMARK 500 14 MET A 154 -78.52 -34.87
REMARK 500 14 HIS A 155 -84.23 32.39
REMARK 500 14 MET A 166 -104.17 46.79
REMARK 500 14 ASP A 167 56.59 33.86
REMARK 500 14 ASN A 171 160.59 95.42
REMARK 500 14 VAL A 176 -74.13 -117.52
REMARK 500 15 SER A 135 -151.44 -70.53
REMARK 500 15 TYR A 149 -70.96 -44.97
REMARK 500 15 MET A 154 -73.42 -34.06
REMARK 500 15 HIS A 155 -84.98 33.07
REMARK 500 15 TYR A 163 -177.54 -176.83
REMARK 500 15 ASP A 167 -29.18 61.65
REMARK 500 15 GLU A 168 -17.85 -170.35
REMARK 500 15 ASN A 170 -157.43 51.55
REMARK 500 15 ASN A 171 169.39 88.37
REMARK 500 15 GLN A 172 -70.46 -105.62
REMARK 500 15 ASN A 181 1.82 -67.84
REMARK 500 16 SER A 135 -168.97 -68.71
REMARK 500 16 MET A 154 -70.67 -32.33
REMARK 500 16 HIS A 155 -75.53 34.67
REMARK 500 16 MET A 166 -169.15 47.61
REMARK 500 16 ASP A 167 -36.90 -176.44
REMARK 500 16 GLU A 168 -60.83 154.48
REMARK 500 16 ASN A 170 -95.83 50.74
REMARK 500 16 ASN A 171 168.88 52.45
REMARK 500 16 GLN A 172 -75.96 -86.51
REMARK 500 16 PHE A 198 95.78 -64.94
REMARK 500 17 TYR A 128 178.89 51.95
REMARK 500 17 SER A 135 -164.79 -76.30
REMARK 500 17 MET A 154 -85.86 -25.54
REMARK 500 17 HIS A 155 -81.02 35.24
REMARK 500 17 MET A 166 91.03 -48.53
REMARK 500 17 TYR A 169 -24.23 -166.92
REMARK 500 17 ASN A 171 -168.33 -171.29
REMARK 500 17 GLN A 172 -75.99 -92.90
REMARK 500 17 ASN A 181 0.92 -68.59
REMARK 500 17 GLU A 196 -177.89 -66.42
REMARK 500 17 PHE A 198 96.67 -67.96
REMARK 500 18 SER A 135 -161.22 -73.46
REMARK 500 18 MET A 154 -81.14 -40.12
REMARK 500 18 HIS A 155 -71.42 38.12
REMARK 500 18 ASN A 159 -41.00 -136.00
REMARK 500 18 ASP A 167 -45.85 -170.73
REMARK 500 18 GLU A 168 -30.36 -166.55
REMARK 500 18 ASN A 170 8.04 43.95
REMARK 500 18 PHE A 175 11.08 -67.45
REMARK 500 18 VAL A 176 -77.80 -121.44
REMARK 500 18 ASN A 181 3.30 -62.58
REMARK 500 18 ASN A 197 61.64 -116.62
REMARK 500 19 SER A 135 -162.92 -73.56
REMARK 500 19 PRO A 137 -166.72 -71.15
REMARK 500 19 MET A 154 -75.21 -37.82
REMARK 500 19 HIS A 155 -98.88 34.50
REMARK 500 19 TYR A 157 131.70 -38.78
REMARK 500 19 ASP A 167 46.65 -74.65
REMARK 500 19 GLU A 168 -15.21 95.85
REMARK 500 19 ASN A 171 -81.03 -174.96
REMARK 500 19 GLN A 172 -63.44 -122.49
REMARK 500 19 PHE A 198 75.80 24.57
REMARK 500 20 MET A 134 -176.86 -66.27
REMARK 500 20 SER A 135 -156.39 -60.05
REMARK 500 20 MET A 154 -75.91 -25.07
REMARK 500 20 HIS A 155 -77.04 34.44
REMARK 500 20 ASN A 159 -44.12 -147.69
REMARK 500 20 ASP A 167 26.85 44.40
REMARK 500 20 GLU A 168 -25.65 62.50
REMARK 500 20 ASN A 170 163.51 -48.30
REMARK 500 20 ASN A 171 -157.99 -154.08
REMARK 500 20 GLN A 172 -75.86 -83.33
REMARK 500 20 GLU A 196 75.57 24.30
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 153 MET A 154 5 -144.93
REMARK 500 GLY A 131 SER A 132 8 -134.93
REMARK 500 MET A 166 ASP A 167 8 -147.79
REMARK 500 ARG A 164 PRO A 165 11 149.24
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 0.08 SIDE CHAIN
REMARK 500 1 PHE A 175 0.08 SIDE CHAIN
REMARK 500 1 ARG A 228 0.09 SIDE CHAIN
REMARK 500 2 PHE A 175 0.09 SIDE CHAIN
REMARK 500 2 ARG A 220 0.08 SIDE CHAIN
REMARK 500 3 TYR A 150 0.08 SIDE CHAIN
REMARK 500 3 TYR A 169 0.08 SIDE CHAIN
REMARK 500 4 ARG A 136 0.09 SIDE CHAIN
REMARK 500 4 PHE A 141 0.09 SIDE CHAIN
REMARK 500 4 ARG A 148 0.11 SIDE CHAIN
REMARK 500 4 TYR A 149 0.09 SIDE CHAIN
REMARK 500 4 ARG A 151 0.12 SIDE CHAIN
REMARK 500 5 PHE A 175 0.08 SIDE CHAIN
REMARK 500 5 ARG A 208 0.09 SIDE CHAIN
REMARK 500 6 TYR A 145 0.06 SIDE CHAIN
REMARK 500 6 ARG A 148 0.08 SIDE CHAIN
REMARK 500 6 ARG A 208 0.12 SIDE CHAIN
REMARK 500 7 ARG A 148 0.08 SIDE CHAIN
REMARK 500 7 ARG A 228 0.10 SIDE CHAIN
REMARK 500 8 ARG A 151 0.10 SIDE CHAIN
REMARK 500 8 ARG A 228 0.08 SIDE CHAIN
REMARK 500 10 TYR A 145 0.07 SIDE CHAIN
REMARK 500 10 ARG A 208 0.13 SIDE CHAIN
REMARK 500 11 TYR A 145 0.07 SIDE CHAIN
REMARK 500 11 ARG A 148 0.08 SIDE CHAIN
REMARK 500 11 TYR A 157 0.09 SIDE CHAIN
REMARK 500 11 TYR A 169 0.07 SIDE CHAIN
REMARK 500 12 ARG A 136 0.13 SIDE CHAIN
REMARK 500 12 TYR A 145 0.08 SIDE CHAIN
REMARK 500 12 TYR A 218 0.08 SIDE CHAIN
REMARK 500 13 ARG A 148 0.13 SIDE CHAIN
REMARK 500 13 ARG A 208 0.10 SIDE CHAIN
REMARK 500 14 ARG A 136 0.12 SIDE CHAIN
REMARK 500 14 TYR A 169 0.07 SIDE CHAIN
REMARK 500 14 ARG A 220 0.10 SIDE CHAIN
REMARK 500 15 TYR A 169 0.09 SIDE CHAIN
REMARK 500 16 TYR A 150 0.10 SIDE CHAIN
REMARK 500 16 TYR A 162 0.07 SIDE CHAIN
REMARK 500 16 ARG A 220 0.08 SIDE CHAIN
REMARK 500 17 TYR A 145 0.07 SIDE CHAIN
REMARK 500 17 TYR A 149 0.09 SIDE CHAIN
REMARK 500 17 PHE A 175 0.10 SIDE CHAIN
REMARK 500 18 TYR A 145 0.13 SIDE CHAIN
REMARK 500 18 TYR A 150 0.09 SIDE CHAIN
REMARK 500 18 ARG A 208 0.08 SIDE CHAIN
REMARK 500 19 TYR A 145 0.07 SIDE CHAIN
REMARK 500 19 ARG A 148 0.08 SIDE CHAIN
REMARK 500 19 TYR A 149 0.11 SIDE CHAIN
REMARK 500 19 ARG A 164 0.08 SIDE CHAIN
REMARK 500 20 TYR A 162 0.07 SIDE CHAIN
REMARK 500 20 TYR A 169 0.08 SIDE CHAIN
REMARK 500 20 ARG A 208 0.08 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CHIRAL CENTERS
REMARK 500
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY
REMARK 500 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,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)
REMARK 500
REMARK 500 M RES CSSEQI IMPROPER EXPECTED FOUND DETAILS
REMARK 500 14 ASP A 167 22.8 L L OUTSIDE RANGE
REMARK 500
REMARK 500 REMARK: NULL
REMARK 650
REMARK 650 HELIX
REMARK 650 DETERMINATION METHOD: AUTHOR PROVIDED.
REMARK 700
REMARK 700 SHEET
REMARK 700 DETERMINATION METHOD: AUTHOR PROVIDED.
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: 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
DBREF 1E1P A 125 228 UNP P78446 P78446 118 221
SEQADV 1E1P ASN A 170 UNP P78446 SER 163 ENGINEERED
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 ASN 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 H1 ASP A 144 MET A 154 1 11
HELIX 2 H2 ASN A 173 LYS A 194 1 22
HELIX 3 H3 GLU A 200 TYR A 226 1 27
SHEET 1 S1 2 TYR A 128 GLY A 131 0
SHEET 2 S1 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 2.03
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 25 2 Bytes