Header list of 1xyw.pdb file
Complete list - r 2 2 Bytes
HEADER UNKNOWN FUNCTION 11-NOV-04 1XYW TITLE ELK PRION PROTEIN COMPND MOL_ID: 1; COMPND 2 MOLECULE: MAJOR PRION PROTEIN; COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: C-TERMINAL DOMAIN; COMPND 5 SYNONYM: PRP; COMPND 6 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: CERVUS ELAPHUS NELSONI; SOURCE 3 ORGANISM_COMMON: AMERICAN ELK; SOURCE 4 ORGANISM_TAXID: 9864; SOURCE 5 STRAIN: NELSONI; SOURCE 6 GENE: PRNP; SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21; SOURCE 8 EXPRESSION_SYSTEM_TAXID: 511693; SOURCE 9 EXPRESSION_SYSTEM_STRAIN: BL21 KEYWDS PRP, CWD, PRION PROTEIN, TSE, UNKNOWN FUNCTION EXPDTA SOLUTION NMR NUMMDL 20 AUTHOR A.D.GOSSERT,S.BONJOUR,D.A.LYSEK,F.FIORITO,K.WUTHRICH REVDAT 5 02-MAR-22 1XYW 1 REMARK REVDAT 4 24-FEB-09 1XYW 1 VERSN REVDAT 3 25-JAN-05 1XYW 1 JRNL REVDAT 2 11-JAN-05 1XYW 1 AUTHOR REVDAT 1 28-DEC-04 1XYW 0 JRNL AUTH A.D.GOSSERT,S.BONJOUR,D.A.LYSEK,F.FIORITO,K.WUTHRICH JRNL TITL PRION PROTEIN NMR STRUCTURES OF ELK AND OF MOUSE/ELK HYBRIDS JRNL REF PROC.NATL.ACAD.SCI.USA V. 102 646 2005 JRNL REFN ISSN 0027-8424 JRNL PMID 15647363 JRNL DOI 10.1073/PNAS.0409008102 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : DYANA 6.2, CANDID 1.0 REMARK 3 AUTHORS : GUENTERT (DYANA), HERRMANN (CANDID) REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 1XYW COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 15-NOV-04. REMARK 100 THE DEPOSITION ID IS D_1000030917. 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 : 1MM EPRP(121-231); 10MM ACETATE REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY; 3D_13C REMARK 210 -SEPARATED_NOESY REMARK 210 SPECTROMETER FIELD STRENGTH : 750 MHZ; 800 MHZ REMARK 210 SPECTROMETER MODEL : DRX; AVANCE 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 : 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 HH TYR A 163 OE1 GLU A 221 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 3 VAL A 184 CA - CB - CG2 ANGL. DEV. = 15.3 DEGREES REMARK 500 5 VAL A 184 CA - CB - CG2 ANGL. DEV. = 11.6 DEGREES REMARK 500 6 VAL A 184 CA - CB - CG2 ANGL. DEV. = 10.6 DEGREES REMARK 500 7 TYR A 163 CB - CG - CD2 ANGL. DEV. = -4.2 DEGREES REMARK 500 7 VAL A 184 CA - CB - CG2 ANGL. DEV. = 11.5 DEGREES REMARK 500 8 TYR A 169 CB - CG - CD2 ANGL. DEV. = -4.7 DEGREES REMARK 500 10 VAL A 184 CA - CB - CG2 ANGL. DEV. = 10.9 DEGREES REMARK 500 11 VAL A 184 CA - CB - CG2 ANGL. DEV. = 15.9 DEGREES REMARK 500 12 TYR A 163 CB - CG - CD2 ANGL. DEV. = -4.3 DEGREES REMARK 500 15 VAL A 184 CA - CB - CG2 ANGL. DEV. = 12.8 DEGREES REMARK 500 16 VAL A 184 CA - CB - CG2 ANGL. DEV. = 9.9 DEGREES REMARK 500 17 VAL A 184 CA - CB - CG2 ANGL. DEV. = 9.8 DEGREES REMARK 500 19 VAL A 184 CA - CB - CG2 ANGL. DEV. = 14.1 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 ARG A 136 140.93 65.29 REMARK 500 1 PHE A 141 -65.08 62.05 REMARK 500 1 ASN A 143 164.99 167.35 REMARK 500 1 ASP A 144 -11.90 -49.44 REMARK 500 1 ASP A 167 -7.97 -55.70 REMARK 500 1 VAL A 189 42.34 -71.38 REMARK 500 1 THR A 190 -46.37 -150.84 REMARK 500 1 GLU A 196 -70.07 -73.29 REMARK 500 1 ASN A 197 -174.47 48.52 REMARK 500 1 TYR A 226 -75.50 -114.95 REMARK 500 1 GLN A 227 58.13 33.57 REMARK 500 2 ARG A 136 141.56 65.09 REMARK 500 2 PHE A 141 -50.28 -141.38 REMARK 500 2 ASN A 143 -166.49 63.84 REMARK 500 2 ASP A 167 -3.33 -41.27 REMARK 500 2 ASN A 170 -62.33 -140.29 REMARK 500 2 THR A 190 -57.34 -146.70 REMARK 500 2 GLN A 227 47.31 34.34 REMARK 500 2 ALA A 230 73.38 45.81 REMARK 500 3 VAL A 122 52.45 37.18 REMARK 500 3 ARG A 136 99.53 65.67 REMARK 500 3 PHE A 141 -16.24 -141.41 REMARK 500 3 ASN A 143 -179.70 -172.02 REMARK 500 3 GLN A 160 -167.89 -123.04 REMARK 500 3 VAL A 189 21.69 -69.14 REMARK 500 3 THR A 190 -50.60 -133.31 REMARK 500 3 ASN A 197 178.62 50.53 REMARK 500 3 TYR A 226 -69.12 -137.29 REMARK 500 3 GLN A 227 54.62 28.22 REMARK 500 3 ALA A 230 108.83 -52.28 REMARK 500 4 ARG A 136 107.76 62.27 REMARK 500 4 PHE A 141 -40.70 58.12 REMARK 500 4 ASN A 143 172.94 138.86 REMARK 500 4 MET A 154 0.32 -66.35 REMARK 500 4 GLN A 160 -160.83 -129.05 REMARK 500 4 PHE A 175 -60.84 -94.01 REMARK 500 4 VAL A 189 33.20 -71.50 REMARK 500 4 THR A 190 -43.10 -141.22 REMARK 500 4 TYR A 226 -58.83 -128.52 REMARK 500 4 GLN A 227 57.60 32.34 REMARK 500 5 ARG A 136 132.02 74.49 REMARK 500 5 ASN A 143 -157.06 60.60 REMARK 500 5 GLN A 160 -167.22 -122.90 REMARK 500 5 ASN A 170 -45.89 -139.62 REMARK 500 5 VAL A 189 17.71 -63.52 REMARK 500 5 THR A 190 -47.85 -145.05 REMARK 500 5 ASN A 197 116.37 -24.94 REMARK 500 5 TYR A 226 -66.97 -127.52 REMARK 500 5 GLN A 227 56.27 26.28 REMARK 500 5 ALA A 230 -22.71 65.04 REMARK 500 REMARK 500 THIS ENTRY HAS 192 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 GLY A 142 ASN A 143 4 -143.73 REMARK 500 ALA A 230 SER A 231 8 148.75 REMARK 500 GLY A 195 GLU A 196 9 148.05 REMARK 500 ARG A 136 PRO A 137 10 146.95 REMARK 500 ARG A 136 PRO A 137 20 148.80 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 ARG A 148 0.08 SIDE CHAIN REMARK 500 1 ARG A 208 0.16 SIDE CHAIN REMARK 500 2 ARG A 148 0.10 SIDE CHAIN REMARK 500 3 ARG A 136 0.14 SIDE CHAIN REMARK 500 3 ARG A 208 0.08 SIDE CHAIN REMARK 500 3 ARG A 220 0.09 SIDE CHAIN REMARK 500 3 ARG A 228 0.08 SIDE CHAIN REMARK 500 4 TYR A 157 0.11 SIDE CHAIN REMARK 500 5 ARG A 156 0.12 SIDE CHAIN REMARK 500 5 TYR A 162 0.07 SIDE CHAIN REMARK 500 6 ARG A 148 0.14 SIDE CHAIN REMARK 500 6 TYR A 149 0.10 SIDE CHAIN REMARK 500 6 TYR A 150 0.15 SIDE CHAIN REMARK 500 6 ARG A 164 0.08 SIDE CHAIN REMARK 500 6 TYR A 218 0.08 SIDE CHAIN REMARK 500 7 TYR A 150 0.09 SIDE CHAIN REMARK 500 7 TYR A 157 0.06 SIDE CHAIN REMARK 500 7 ARG A 164 0.08 SIDE CHAIN REMARK 500 8 ARG A 148 0.11 SIDE CHAIN REMARK 500 8 TYR A 157 0.11 SIDE CHAIN REMARK 500 8 TYR A 162 0.10 SIDE CHAIN REMARK 500 8 TYR A 169 0.07 SIDE CHAIN REMARK 500 8 TYR A 226 0.08 SIDE CHAIN REMARK 500 9 ARG A 136 0.10 SIDE CHAIN REMARK 500 9 TYR A 150 0.08 SIDE CHAIN REMARK 500 9 TYR A 162 0.08 SIDE CHAIN REMARK 500 9 ARG A 220 0.12 SIDE CHAIN REMARK 500 10 PHE A 175 0.08 SIDE CHAIN REMARK 500 10 ARG A 220 0.11 SIDE CHAIN REMARK 500 11 ARG A 148 0.08 SIDE CHAIN REMARK 500 11 TYR A 150 0.07 SIDE CHAIN REMARK 500 11 ARG A 151 0.09 SIDE CHAIN REMARK 500 11 TYR A 155 0.10 SIDE CHAIN REMARK 500 11 TYR A 157 0.08 SIDE CHAIN REMARK 500 11 ARG A 208 0.08 SIDE CHAIN REMARK 500 12 ARG A 136 0.11 SIDE CHAIN REMARK 500 12 ARG A 148 0.09 SIDE CHAIN REMARK 500 12 TYR A 163 0.07 SIDE CHAIN REMARK 500 13 ARG A 136 0.09 SIDE CHAIN REMARK 500 13 ARG A 148 0.17 SIDE CHAIN REMARK 500 14 TYR A 149 0.14 SIDE CHAIN REMARK 500 14 ARG A 151 0.09 SIDE CHAIN REMARK 500 14 TYR A 155 0.07 SIDE CHAIN REMARK 500 14 ARG A 156 0.09 SIDE CHAIN REMARK 500 14 TYR A 169 0.07 SIDE CHAIN REMARK 500 15 TYR A 155 0.12 SIDE CHAIN REMARK 500 16 ARG A 151 0.13 SIDE CHAIN REMARK 500 16 TYR A 155 0.08 SIDE CHAIN REMARK 500 16 ARG A 228 0.09 SIDE CHAIN REMARK 500 17 ARG A 136 0.12 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: 6383 RELATED DB: BMRB DBREF 1XYW A 121 231 UNP P67986 PRIO_CEREN 124 234 SEQRES 1 A 111 VAL VAL GLY GLY LEU GLY GLY TYR MET LEU GLY SER ALA SEQRES 2 A 111 MET SER ARG PRO LEU ILE HIS PHE GLY ASN ASP TYR GLU SEQRES 3 A 111 ASP ARG TYR TYR ARG GLU ASN MET TYR ARG TYR PRO ASN SEQRES 4 A 111 GLN VAL TYR TYR ARG PRO VAL ASP GLN TYR ASN ASN GLN SEQRES 5 A 111 ASN THR PHE VAL HIS ASP CYS VAL ASN ILE THR VAL LYS SEQRES 6 A 111 GLN HIS THR VAL THR THR THR THR LYS GLY GLU ASN PHE SEQRES 7 A 111 THR GLU THR ASP ILE LYS MET MET GLU ARG VAL VAL GLU SEQRES 8 A 111 GLN MET CYS ILE THR GLN TYR GLN ARG GLU SER GLU ALA SEQRES 9 A 111 TYR TYR GLN ARG GLY ALA SER HELIX 1 1 ASN A 143 MET A 154 1 12 HELIX 2 2 TYR A 155 TYR A 157 5 3 HELIX 3 3 PRO A 165 TYR A 169 5 5 HELIX 4 4 ASN A 171 THR A 192 1 22 HELIX 5 5 THR A 199 TYR A 225 1 27 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 2.04 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