Header list of 1u3m.pdb file
Complete list - r 2 2 Bytes
HEADER MEMBRANE PROTEIN 22-JUL-04 1U3M TITLE NMR STRUCTURE OF THE CHICKEN PRION PROTEIN FRAGMENT 128-242 COMPND MOL_ID: 1; COMPND 2 MOLECULE: PRION-LIKE PROTEIN; COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: C-TERMINAL DOMAIN; COMPND 5 SYNONYM: CHPRP; COMPND 6 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: GALLUS GALLUS; SOURCE 3 ORGANISM_COMMON: CHICKEN; SOURCE 4 ORGANISM_TAXID: 9031; 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, TSE, PRP, MEMBRANE PROTEIN EXPDTA SOLUTION NMR NUMMDL 20 AUTHOR D.A.LYSEK,L.CALZOLAI,P.GUNTERT,K.WUTHRICH REVDAT 5 02-MAR-22 1U3M 1 REMARK SEQADV REVDAT 4 24-FEB-09 1U3M 1 VERSN REVDAT 3 25-JAN-05 1U3M 1 JRNL REVDAT 2 11-JAN-05 1U3M 1 AUTHOR JRNL REVDAT 1 04-JAN-05 1U3M 0 JRNL AUTH L.CALZOLAI,D.A.LYSEK,D.R.PEREZ,P.GUNTERT,K.WUTHRICH JRNL TITL PRION PROTEIN NMR STRUCTURES OF CHICKENS, TURTLES, AND FROGS 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 2012 RESTRAINTS, 1889 ARE REMARK 3 NOE-DERIVED REMARK 3 DISTANCE CONSTRAINTS, 123 DIHEDRAL ANGLE RESTRAINTS REMARK 4 REMARK 4 1U3M COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 26-JUL-04. REMARK 100 THE DEPOSITION ID IS D_1000023202. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 292 REMARK 210 PH : 4.3 REMARK 210 IONIC STRENGTH : 10MM REMARK 210 PRESSURE : AMBIENT REMARK 210 SAMPLE CONTENTS : 1MM CHICKEN PRION PROTEIN REMARK 210 (CHPRP(128-242)) U-15N, 13C; REMARK 210 10MM SODIUM ACETATE; 95% H2O, 5% REMARK 210 D2O; OR 99% D2O REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_13C-SEPARATED_NOESY; 3D_15N 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: THE STRUCTURE WAS DETERMINED USING TRIPLE-RESONANCE NMR REMARK 210 SPECTROSCOPY. 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 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 7 VAL A 168 CG1 - CB - CG2 ANGL. DEV. = -9.9 DEGREES REMARK 500 9 CYS A 186 CA - CB - SG ANGL. DEV. = 7.4 DEGREES REMARK 500 9 ARG A 228 CD - NE - CZ ANGL. DEV. = 9.3 DEGREES REMARK 500 15 ARG A 163 NE - CZ - NH2 ANGL. DEV. = -3.7 DEGREES REMARK 500 16 VAL A 226 CA - CB - CG2 ANGL. DEV. = 10.0 DEGREES REMARK 500 18 TYR A 154 CB - CG - CD2 ANGL. DEV. = -3.9 DEGREES REMARK 500 19 VAL A 223 CA - CB - CG2 ANGL. DEV. = 12.9 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 VAL A 128 169.58 67.17 REMARK 500 1 VAL A 129 -48.43 74.97 REMARK 500 1 HIS A 147 -74.66 -89.51 REMARK 500 1 PHE A 148 82.78 26.84 REMARK 500 1 ARG A 163 -43.66 -132.84 REMARK 500 1 TYR A 164 85.78 25.16 REMARK 500 1 ASN A 166 -6.46 53.72 REMARK 500 1 SER A 175 -54.56 118.97 REMARK 500 1 ALA A 200 -103.55 -119.54 REMARK 500 1 LYS A 202 -99.32 51.87 REMARK 500 1 ASN A 203 29.70 -168.78 REMARK 500 1 THR A 204 -159.41 -107.12 REMARK 500 1 ALA A 210 -55.92 -158.01 REMARK 500 1 ASN A 212 108.51 64.92 REMARK 500 2 VAL A 128 71.55 52.91 REMARK 500 2 VAL A 129 -55.18 -148.34 REMARK 500 2 MET A 144 -164.36 -79.12 REMARK 500 2 TYR A 146 -37.46 -163.03 REMARK 500 2 HIS A 147 -91.24 73.04 REMARK 500 2 PHE A 148 71.94 48.07 REMARK 500 2 ARG A 163 -54.48 -138.53 REMARK 500 2 TYR A 164 80.30 34.30 REMARK 500 2 ASN A 166 -3.31 50.93 REMARK 500 2 ASP A 172 81.08 66.48 REMARK 500 2 SER A 175 -40.98 122.31 REMARK 500 2 PRO A 198 -9.28 -58.58 REMARK 500 2 LYS A 201 44.35 -144.95 REMARK 500 2 ASN A 203 50.71 -175.70 REMARK 500 2 GLU A 206 -71.82 -96.58 REMARK 500 2 ALA A 209 -52.60 69.10 REMARK 500 2 ALA A 210 -74.49 54.54 REMARK 500 2 ASN A 212 107.27 -173.61 REMARK 500 3 VAL A 129 -35.80 -177.00 REMARK 500 3 LEU A 132 106.76 108.96 REMARK 500 3 TYR A 146 82.59 32.99 REMARK 500 3 HIS A 147 -86.43 -48.18 REMARK 500 3 TYR A 164 74.12 15.78 REMARK 500 3 ASN A 166 -16.22 53.42 REMARK 500 3 SER A 175 -59.82 157.01 REMARK 500 3 ALA A 207 -83.34 -132.93 REMARK 500 3 ALA A 211 50.79 -142.86 REMARK 500 3 ASN A 212 117.84 78.90 REMARK 500 3 LEU A 240 -66.42 -90.24 REMARK 500 3 ALA A 241 -21.12 64.46 REMARK 500 4 SER A 127 -82.56 -142.57 REMARK 500 4 LEU A 132 -33.91 -132.39 REMARK 500 4 HIS A 147 -93.31 -89.89 REMARK 500 4 TYR A 164 70.99 27.94 REMARK 500 4 ASN A 166 4.98 48.04 REMARK 500 4 SER A 175 -28.92 117.86 REMARK 500 REMARK 500 THIS ENTRY HAS 345 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 203 THR A 204 1 -148.24 REMARK 500 ALA A 241 SER A 242 1 137.48 REMARK 500 THR A 204 SER A 205 12 146.25 REMARK 500 ALA A 241 SER A 242 14 143.76 REMARK 500 SER A 142 GLY A 143 17 145.04 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 135 0.08 SIDE CHAIN REMARK 500 1 TYR A 154 0.08 SIDE CHAIN REMARK 500 1 ARG A 163 0.08 SIDE CHAIN REMARK 500 2 ARG A 155 0.10 SIDE CHAIN REMARK 500 2 ARG A 167 0.10 SIDE CHAIN REMARK 500 3 ARG A 171 0.10 SIDE CHAIN REMARK 500 3 ARG A 228 0.21 SIDE CHAIN REMARK 500 4 TYR A 154 0.07 SIDE CHAIN REMARK 500 4 ARG A 228 0.16 SIDE CHAIN REMARK 500 5 TYR A 173 0.09 SIDE CHAIN REMARK 500 5 TYR A 235 0.10 SIDE CHAIN REMARK 500 5 ARG A 236 0.09 SIDE CHAIN REMARK 500 5 ARG A 239 0.09 SIDE CHAIN REMARK 500 7 ARG A 155 0.19 SIDE CHAIN REMARK 500 7 ARG A 236 0.09 SIDE CHAIN REMARK 500 8 TYR A 169 0.08 SIDE CHAIN REMARK 500 8 TYR A 173 0.08 SIDE CHAIN REMARK 500 8 ARG A 239 0.08 SIDE CHAIN REMARK 500 9 TYR A 146 0.07 SIDE CHAIN REMARK 500 9 ARG A 150 0.08 SIDE CHAIN REMARK 500 9 ARG A 163 0.08 SIDE CHAIN REMARK 500 10 ARG A 236 0.08 SIDE CHAIN REMARK 500 11 ARG A 155 0.09 SIDE CHAIN REMARK 500 12 ARG A 171 0.17 SIDE CHAIN REMARK 500 12 TYR A 194 0.07 SIDE CHAIN REMARK 500 12 ARG A 228 0.10 SIDE CHAIN REMARK 500 13 ARG A 171 0.09 SIDE CHAIN REMARK 500 13 ARG A 239 0.09 SIDE CHAIN REMARK 500 14 TYR A 170 0.08 SIDE CHAIN REMARK 500 14 TYR A 238 0.08 SIDE CHAIN REMARK 500 15 ARG A 163 0.08 SIDE CHAIN REMARK 500 15 TYR A 164 0.15 SIDE CHAIN REMARK 500 15 TYR A 173 0.09 SIDE CHAIN REMARK 500 16 TYR A 146 0.09 SIDE CHAIN REMARK 500 16 ARG A 155 0.09 SIDE CHAIN REMARK 500 16 TYR A 194 0.07 SIDE CHAIN REMARK 500 17 TYR A 169 0.11 SIDE CHAIN REMARK 500 18 ARG A 167 0.11 SIDE CHAIN REMARK 500 18 TYR A 170 0.12 SIDE CHAIN REMARK 500 19 ARG A 150 0.08 SIDE CHAIN REMARK 500 19 ARG A 228 0.08 SIDE CHAIN REMARK 500 20 TYR A 194 0.07 SIDE CHAIN REMARK 500 REMARK 500 REMARK: NULL DBREF 1U3M A 128 242 UNP P27177 PRIO_CHICK 128 242 SEQADV 1U3M GLY A 126 UNP P27177 CLONING ARTIFACT SEQADV 1U3M SER A 127 UNP P27177 CLONING ARTIFACT SEQRES 1 A 117 GLY SER VAL VAL GLY GLY LEU GLY GLY TYR ALA MET GLY SEQRES 2 A 117 ARG VAL MET SER GLY MET ASN TYR HIS PHE ASP ARG PRO SEQRES 3 A 117 ASP GLU TYR ARG TRP TRP SER GLU ASN SER ALA ARG TYR SEQRES 4 A 117 PRO ASN ARG VAL TYR TYR ARG ASP TYR SER SER PRO VAL SEQRES 5 A 117 PRO GLN ASP VAL PHE VAL ALA ASP CYS PHE ASN ILE THR SEQRES 6 A 117 VAL THR GLU TYR SER ILE GLY PRO ALA ALA LYS LYS ASN SEQRES 7 A 117 THR SER GLU ALA VAL ALA ALA ALA ASN GLN THR GLU VAL SEQRES 8 A 117 GLU MET GLU ASN LYS VAL VAL THR LYS VAL ILE ARG GLU SEQRES 9 A 117 MET CYS VAL GLN GLN TYR ARG GLU TYR ARG LEU ALA SER HELIX 1 1 ARG A 150 ALA A 162 1 13 HELIX 2 2 PRO A 178 SER A 195 1 18 HELIX 3 3 ASN A 212 ALA A 241 1 30 SHEET 1 A 2 ALA A 136 MET A 137 0 SHEET 2 A 2 TYR A 169 TYR A 170 -1 O TYR A 170 N ALA A 136 SSBOND 1 CYS A 186 CYS A 231 1555 1555 2.05 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