Header list of 1u5l.pdb file
Complete list - r 2 2 Bytes
HEADER MEMBRANE PROTEIN 28-JUL-04 1U5L TITLE SOLUTION STRUCTURE OF THE TURTLE PRION PROTEIN FRAGMENT (121-226) COMPND MOL_ID: 1; COMPND 2 MOLECULE: PRION PROTEIN; COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: C-TERMINAL DOMAIN (RESIDUES 121-226); COMPND 5 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: TRACHEMYS SCRIPTA; SOURCE 3 ORGANISM_COMMON: RED-EARED SLIDER TURTLE; SOURCE 4 ORGANISM_TAXID: 34903; 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 PRNP, PRP, PRION, TSE, MEMBRANE PROTEIN EXPDTA SOLUTION NMR NUMMDL 20 AUTHOR D.A.LYSEK,L.CALZOLAI,P.GUNTERT,K.WUTHRICH REVDAT 5 02-MAR-22 1U5L 1 REMARK SEQADV REVDAT 4 24-FEB-09 1U5L 1 VERSN REVDAT 3 25-JAN-05 1U5L 1 JRNL REVDAT 2 11-JAN-05 1U5L 1 JRNL AUTHOR REVDAT 1 04-JAN-05 1U5L 0 JRNL AUTH L.CALZOLAI,D.A.LYSEK,D.R.PEREZ,P.GUNTERT,K.WUTHRICH JRNL TITL PRION PROTEIN NMR STRUCTURES OF CHICKEN, TURTLE, AND FROG JRNL REF PROC.NATL.ACAD.SCI.USA V. 102 651 2005 JRNL REFN ISSN 0027-8424 JRNL PMID 15647366 JRNL DOI 10.1073/PNAS.0408939102 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : DYANA 6.0, DYANA 6.0 REMARK 3 AUTHORS : GUENTERT (DYANA), GUENTERT (DYANA) REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: REMARK 3 THE STRUCTURES ARE BASED ON A TOTAL OF 1632 RESTRAINTS, 1522 ARE REMARK 3 NOE-DERIVED REMARK 3 DISTANCE CONSTRAINTS, 110 DIHEDRAL ANGLE RESTRAINTS, 109 REMARK 4 REMARK 4 1U5L COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 30-JUL-04. REMARK 100 THE DEPOSITION ID IS D_1000023273. 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 : 10MM REMARK 210 PRESSURE : AMBIENT REMARK 210 SAMPLE CONTENTS : 0.5MM TURTLE PRION PROTEIN U REMARK 210 -15N,13C; 10MM SODIUM ACETATE, REMARK 210 90% H2O, 10% D2O; 0.5MM TURTLE REMARK 210 PRION PROTEIN U-15N,13C; 10MM REMARK 210 SODIUM ACETATE, 99% D2O REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY; 3D_13C REMARK 210 -SEPARATED_NOESY REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 600 MHZ; 750 MHZ REMARK 210 SPECTROMETER MODEL : DRX 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 : STRUCTURES WITH THE LEAST REMARK 210 RESTRAINT VIOLATIONS REMARK 210 REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1 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 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 465 REMARK 465 MISSING RESIDUES REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE REMARK 465 EXPERIMENT. (RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 465 SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.) REMARK 465 MODELS 1-20 REMARK 465 RES C SSSEQI REMARK 465 GLY A 226 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 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 ARG A 143 NE - CZ - NH2 ANGL. DEV. = -3.0 DEGREES REMARK 500 2 VAL A 203 CA - CB - CG2 ANGL. DEV. = 9.4 DEGREES REMARK 500 3 VAL A 181 CA - CB - CG2 ANGL. DEV. = 9.9 DEGREES REMARK 500 4 TYR A 188 CB - CG - CD2 ANGL. DEV. = -4.1 DEGREES REMARK 500 7 VAL A 181 CA - CB - CG2 ANGL. DEV. = 9.1 DEGREES REMARK 500 7 VAL A 203 CA - CB - CG2 ANGL. DEV. = 9.8 DEGREES REMARK 500 10 CYS A 180 CA - CB - SG ANGL. DEV. = 6.8 DEGREES REMARK 500 13 VAL A 181 CA - CB - CG2 ANGL. DEV. = 9.3 DEGREES REMARK 500 15 TYR A 166 CB - CG - CD2 ANGL. DEV. = -4.2 DEGREES REMARK 500 16 TYR A 188 CB - CG - CD2 ANGL. DEV. = -4.0 DEGREES REMARK 500 19 TYR A 188 CB - CG - CD2 ANGL. DEV. = -4.1 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 67.89 -174.88 REMARK 500 1 LEU A 125 -95.98 -34.51 REMARK 500 1 MET A 134 -76.49 -38.96 REMARK 500 1 SER A 135 138.15 145.80 REMARK 500 1 PHE A 141 149.91 66.57 REMARK 500 1 ASN A 153 -108.70 70.04 REMARK 500 1 SER A 154 -45.57 32.38 REMARK 500 1 ARG A 156 6.34 -68.19 REMARK 500 1 TYR A 157 171.49 61.20 REMARK 500 1 ASN A 159 30.34 -87.53 REMARK 500 1 ARG A 169 1.95 42.76 REMARK 500 1 GLU A 173 0.71 -58.65 REMARK 500 1 GLU A 194 -57.27 -138.71 REMARK 500 1 GLN A 196 -4.14 67.79 REMARK 500 1 GLN A 200 0.58 -68.57 REMARK 500 1 LYS A 207 -65.83 -93.39 REMARK 500 2 SER A 132 -72.48 -173.98 REMARK 500 2 ALA A 133 73.98 60.34 REMARK 500 2 SER A 135 102.43 56.14 REMARK 500 2 MET A 137 151.75 61.74 REMARK 500 2 PHE A 141 179.08 58.44 REMARK 500 2 ASN A 159 39.37 -79.81 REMARK 500 2 ARG A 169 25.23 43.25 REMARK 500 2 LYS A 189 73.68 36.30 REMARK 500 2 GLN A 196 -62.13 166.81 REMARK 500 2 ASN A 197 71.12 172.17 REMARK 500 2 MET A 206 1.45 -68.59 REMARK 500 2 LYS A 207 -66.63 -92.92 REMARK 500 3 VAL A 122 106.90 49.76 REMARK 500 3 LEU A 125 118.80 77.55 REMARK 500 3 SER A 132 -67.73 61.98 REMARK 500 3 ALA A 133 84.95 51.20 REMARK 500 3 SER A 135 11.32 53.09 REMARK 500 3 PHE A 141 -171.93 49.23 REMARK 500 3 PRO A 158 -159.73 -79.70 REMARK 500 3 TYR A 166 98.94 28.96 REMARK 500 3 GLN A 196 -6.41 55.74 REMARK 500 4 VAL A 121 65.22 28.72 REMARK 500 4 SER A 135 105.61 10.91 REMARK 500 4 PHE A 141 179.99 59.25 REMARK 500 4 ASN A 153 48.26 -90.68 REMARK 500 4 SER A 154 -54.04 16.16 REMARK 500 4 ASN A 155 12.14 -163.54 REMARK 500 4 TYR A 166 -147.04 -73.77 REMARK 500 4 ASN A 167 -3.18 -141.26 REMARK 500 4 LYS A 189 73.43 42.40 REMARK 500 4 GLN A 196 12.90 56.22 REMARK 500 4 ASN A 197 34.63 -143.40 REMARK 500 5 VAL A 121 45.73 -147.38 REMARK 500 5 LEU A 125 74.85 54.03 REMARK 500 REMARK 500 THIS ENTRY HAS 260 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 224 SER A 225 11 -148.51 REMARK 500 GLY A 136 MET A 137 12 -147.46 REMARK 500 VAL A 171 PRO A 172 17 149.00 REMARK 500 LYS A 164 GLU A 165 18 145.76 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 163 0.06 SIDE CHAIN REMARK 500 1 ARG A 178 0.11 SIDE CHAIN REMARK 500 2 TYR A 166 0.08 SIDE CHAIN REMARK 500 2 TYR A 188 0.07 SIDE CHAIN REMARK 500 3 ARG A 169 0.13 SIDE CHAIN REMARK 500 3 TYR A 221 0.07 SIDE CHAIN REMARK 500 5 TYR A 218 0.07 SIDE CHAIN REMARK 500 5 TYR A 221 0.09 SIDE CHAIN REMARK 500 6 TYR A 166 0.09 SIDE CHAIN REMARK 500 7 TYR A 166 0.08 SIDE CHAIN REMARK 500 7 ARG A 169 0.08 SIDE CHAIN REMARK 500 7 ARG A 178 0.09 SIDE CHAIN REMARK 500 7 TYR A 218 0.07 SIDE CHAIN REMARK 500 8 ARG A 156 0.12 SIDE CHAIN REMARK 500 8 TYR A 163 0.07 SIDE CHAIN REMARK 500 9 TYR A 221 0.09 SIDE CHAIN REMARK 500 10 TYR A 163 0.07 SIDE CHAIN REMARK 500 10 ARG A 169 0.10 SIDE CHAIN REMARK 500 10 TYR A 218 0.09 SIDE CHAIN REMARK 500 11 ARG A 143 0.08 SIDE CHAIN REMARK 500 11 TYR A 157 0.09 SIDE CHAIN REMARK 500 12 TYR A 163 0.08 SIDE CHAIN REMARK 500 12 ARG A 204 0.11 SIDE CHAIN REMARK 500 13 TYR A 128 0.08 SIDE CHAIN REMARK 500 13 ARG A 147 0.10 SIDE CHAIN REMARK 500 15 TYR A 221 0.11 SIDE CHAIN REMARK 500 16 ARG A 147 0.07 SIDE CHAIN REMARK 500 16 TYR A 218 0.07 SIDE CHAIN REMARK 500 16 TYR A 221 0.11 SIDE CHAIN REMARK 500 17 TYR A 128 0.09 SIDE CHAIN REMARK 500 17 ARG A 147 0.11 SIDE CHAIN REMARK 500 17 TYR A 218 0.06 SIDE CHAIN REMARK 500 19 TYR A 128 0.07 SIDE CHAIN REMARK 500 19 ARG A 147 0.08 SIDE CHAIN REMARK 500 20 TYR A 162 0.09 SIDE CHAIN REMARK 500 20 TYR A 166 0.07 SIDE CHAIN REMARK 500 20 TYR A 218 0.07 SIDE CHAIN REMARK 500 REMARK 500 REMARK: NULL DBREF 1U5L A 121 226 UNP Q9I9C0 Q9I9C0_TRASC 143 248 SEQADV 1U5L GLY A 119 UNP Q9I9C0 CLONING ARTIFACT SEQADV 1U5L SER A 120 UNP Q9I9C0 CLONING ARTIFACT SEQADV 1U5L VAL A 181 UNP Q9I9C0 LEU 203 SEE REMARK 999 SEQADV 1U5L ILE A 183 UNP Q9I9C0 ASN 205 SEE REMARK 999 SEQRES 1 A 108 GLY SER VAL VAL GLY GLY LEU GLY GLY TYR ALA LEU GLY SEQRES 2 A 108 SER ALA MET SER GLY MET ARG MET ASN PHE ASP ARG PRO SEQRES 3 A 108 GLU GLU ARG GLN TRP TRP ASN GLU ASN SER ASN ARG TYR SEQRES 4 A 108 PRO ASN GLN VAL TYR TYR LYS GLU TYR ASN ASP ARG SER SEQRES 5 A 108 VAL PRO GLU GLY ARG PHE VAL ARG ASP CYS VAL ASN ILE SEQRES 6 A 108 THR VAL THR GLU TYR LYS ILE ASP PRO ASN GLU ASN GLN SEQRES 7 A 108 ASN VAL THR GLN VAL GLU VAL ARG VAL MET LYS GLN VAL SEQRES 8 A 108 ILE GLN GLU MET CYS MET GLN GLN TYR GLN GLN TYR GLN SEQRES 9 A 108 LEU ALA SER GLY HELIX 1 1 ARG A 143 ASN A 153 1 11 HELIX 2 2 GLY A 174 TYR A 188 1 15 HELIX 3 3 THR A 199 SER A 225 1 27 SHEET 1 A 2 ALA A 129 LEU A 130 0 SHEET 2 A 2 TYR A 162 TYR A 163 -1 O TYR A 163 N ALA A 129 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