Header list of 1d6k.pdb file
Complete list - r 23 2 Bytes
HEADER RIBOSOME 14-OCT-99 1D6K TITLE NMR SOLUTION STRUCTURE OF THE 5S RRNA E-LOOP/L25 COMPLEX COMPND MOL_ID: 1; COMPND 2 MOLECULE: 5S RRNA E-LOOP (5SE); COMPND 3 CHAIN: B; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: RIBOSOMAL PROTEIN L25; COMPND 7 CHAIN: A; COMPND 8 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 SYNTHETIC: YES; SOURCE 3 OTHER_DETAILS: THE RNA SEQUENCE WAS SYNTHESIZED VIA IN VITRO SOURCE 4 TRANSCIPTION (T7 POLYMERASE) OF A PLASMID DNA TEMPLATE.; SOURCE 5 MOL_ID: 2; SOURCE 6 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI; SOURCE 7 ORGANISM_TAXID: 562; SOURCE 8 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 9 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 11 EXPRESSION_SYSTEM_PLASMID: PET11A KEYWDS PROTEIN-RNA COMPLEX, RIBOSOME EXPDTA SOLUTION NMR NUMMDL 20 AUTHOR M.STOLDT,J.WOHNERT,O.OHLENSCHLAGER,M.GORLACH,L.R.BROWN REVDAT 4 23-MAR-22 1D6K 1 REMARK REVDAT 3 24-FEB-09 1D6K 1 VERSN REVDAT 2 29-NOV-99 1D6K 1 EXPDTA REVDAT 1 22-NOV-99 1D6K 0 JRNL AUTH M.STOLDT,J.WOHNERT,O.OHLENSCHLAGER,M.GORLACH,L.R.BROWN JRNL TITL THE NMR STRUCTURE OF THE 5S RRNA E-DOMAIN-PROTEIN L25 JRNL TITL 2 COMPLEX SHOWS PREFORMED AND INDUCED RECOGNITION. JRNL REF EMBO J. V. 18 6508 1999 JRNL REFN ISSN 0261-4189 JRNL PMID 10562563 JRNL DOI 10.1093/EMBOJ/18.22.6508 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : VNMR 5.3B, OPAL/AMBER94 2.6 REMARK 3 AUTHORS : LUGINBUEHL/CORNELL (OPAL/AMBER94) REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 1D6K COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 14-OCT-99. REMARK 100 THE DEPOSITION ID IS D_1000009836. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 298; 298; 298; 298; 298; 298 REMARK 210 PH : 7.2; 7.2; 7.2; 7.2; 7.2; 7.2 REMARK 210 IONIC STRENGTH : 100MM KCL; 100MM KCL; 100MM KCL; REMARK 210 100MM KCL; 100MM KCL; 100MM KCL REMARK 210 PRESSURE : AMBIENT; AMBIENT; AMBIENT; REMARK 210 AMBIENT; AMBIENT; AMBIENT REMARK 210 SAMPLE CONTENTS : 2MM L25 U-15N,13C/5SE NA; 20MM REMARK 210 PHOSPHATE BUFFER; 100MM KCL; REMARK 210 2.2MM L25 U-15N,13C/5SE NA; 20MM REMARK 210 PHOSPHATE BUFFER; 100MM KCL; REMARK 210 1.8MM L25 NA/5SE U-15N; 20MM REMARK 210 PHOSPHATE BUFFER; 100MM KCL; 1MM REMARK 210 L25 U-15N/5SE U-15N; 20MM REMARK 210 PHOSPHATE BUFFER; 100MM KCL; REMARK 210 1.8MM L25 NA/5SE U-15N,13C; 20MM REMARK 210 PHOSPHATE BUFFER; 100MM KCL; REMARK 210 1.7MM L25 NA/5SE U-15N,13C; 20MM REMARK 210 PHOSPHATE BUFFER; 100MM KCL REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_13C-SEPARATED_NOESY; 3D_15N REMARK 210 -SEPARATED_NOESY; 3D_F1-13C-FILTERED,F3-EDITED_NOESY; 2D NOESY; REMARK 210 2D_CPMG_NOESY; 3D_F1-13C/15N-FILTERED,F3-EDITED_NOESY REMARK 210 SPECTROMETER FIELD STRENGTH : 750 MHZ REMARK 210 SPECTROMETER MODEL : INOVA REMARK 210 SPECTROMETER MANUFACTURER : VARIAN REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : XEASY 1.3.9, DYANA 1.5 REMARK 210 METHOD USED : HYBRID DISTANCE REMARK 210 GEOMETRY/SIMULATED ANNEALING REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 200 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20 REMARK 210 CONFORMERS, SELECTION CRITERIA : TARGET FUNCTION REMARK 210 REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 2 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: DIMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, 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 1 C B 271 O4' - C1' - N1 ANGL. DEV. = 6.0 DEGREES REMARK 500 1 A B 273 O4' - C1' - N9 ANGL. DEV. = 4.5 DEGREES REMARK 500 1 U B 274 O4' - C1' - N1 ANGL. DEV. = 4.6 DEGREES REMARK 500 1 U B 277 O4' - C1' - N1 ANGL. DEV. = 4.5 DEGREES REMARK 500 1 U B 280 O4' - C1' - N1 ANGL. DEV. = 6.0 DEGREES REMARK 500 1 C B 283 O4' - C1' - N1 ANGL. DEV. = 4.5 DEGREES REMARK 500 1 U B 285 C3' - O3' - P ANGL. DEV. = 7.2 DEGREES REMARK 500 1 G B 292 C2 - N3 - C4 ANGL. DEV. = 3.1 DEGREES REMARK 500 1 G B 292 N3 - C4 - C5 ANGL. DEV. = -3.2 DEGREES REMARK 500 1 G B 293 O4' - C1' - N9 ANGL. DEV. = 4.7 DEGREES REMARK 500 1 U B 295 O4' - C1' - N1 ANGL. DEV. = 5.3 DEGREES REMARK 500 1 C B 297 O4' - C1' - N1 ANGL. DEV. = 5.0 DEGREES REMARK 500 1 G B 305 O4' - C1' - N9 ANGL. DEV. = 4.6 DEGREES REMARK 500 1 TYR A 31 CB - CG - CD2 ANGL. DEV. = -3.9 DEGREES REMARK 500 2 C B 270 O4' - C1' - N1 ANGL. DEV. = 4.4 DEGREES REMARK 500 2 C B 271 O4' - C1' - N1 ANGL. DEV. = 5.8 DEGREES REMARK 500 2 U B 274 O4' - C1' - N1 ANGL. DEV. = 4.3 DEGREES REMARK 500 2 U B 277 O4' - C1' - N1 ANGL. DEV. = 4.3 DEGREES REMARK 500 2 U B 280 O4' - C1' - N1 ANGL. DEV. = 5.6 DEGREES REMARK 500 2 U B 282 O4' - C1' - N1 ANGL. DEV. = 4.4 DEGREES REMARK 500 2 C B 283 O4' - C1' - N1 ANGL. DEV. = 5.4 DEGREES REMARK 500 2 G B 292 N3 - C4 - C5 ANGL. DEV. = -3.0 DEGREES REMARK 500 2 U B 295 O4' - C1' - N1 ANGL. DEV. = 5.6 DEGREES REMARK 500 2 C B 297 O4' - C1' - N1 ANGL. DEV. = 4.6 DEGREES REMARK 500 3 C B 270 O4' - C1' - N1 ANGL. DEV. = 4.4 DEGREES REMARK 500 3 C B 271 O4' - C1' - N1 ANGL. DEV. = 6.0 DEGREES REMARK 500 3 U B 274 O4' - C1' - N1 ANGL. DEV. = 5.0 DEGREES REMARK 500 3 U B 277 O4' - C1' - N1 ANGL. DEV. = 4.4 DEGREES REMARK 500 3 U B 280 O4' - C1' - N1 ANGL. DEV. = 4.5 DEGREES REMARK 500 3 U B 282 O4' - C1' - N1 ANGL. DEV. = 4.3 DEGREES REMARK 500 3 U B 295 O4' - C1' - N1 ANGL. DEV. = 4.7 DEGREES REMARK 500 3 C B 297 O4' - C1' - N1 ANGL. DEV. = 5.2 DEGREES REMARK 500 3 U B 307 O4' - C1' - N1 ANGL. DEV. = 4.7 DEGREES REMARK 500 3 ARG A 9 NE - CZ - NH1 ANGL. DEV. = 3.4 DEGREES REMARK 500 4 G B 267 O4' - C1' - N9 ANGL. DEV. = 6.3 DEGREES REMARK 500 4 C B 270 O4' - C1' - N1 ANGL. DEV. = 4.8 DEGREES REMARK 500 4 C B 271 O4' - C1' - N1 ANGL. DEV. = 6.5 DEGREES REMARK 500 4 U B 274 O4' - C1' - N1 ANGL. DEV. = 4.6 DEGREES REMARK 500 4 U B 277 O4' - C1' - N1 ANGL. DEV. = 4.8 DEGREES REMARK 500 4 U B 280 O4' - C1' - N1 ANGL. DEV. = 6.0 DEGREES REMARK 500 4 C B 283 O4' - C1' - N1 ANGL. DEV. = 4.3 DEGREES REMARK 500 4 G B 292 O4' - C1' - N9 ANGL. DEV. = 4.4 DEGREES REMARK 500 4 G B 292 C2 - N3 - C4 ANGL. DEV. = 3.0 DEGREES REMARK 500 4 G B 292 N3 - C4 - C5 ANGL. DEV. = -3.1 DEGREES REMARK 500 4 G B 293 O4' - C1' - N9 ANGL. DEV. = 5.2 DEGREES REMARK 500 4 U B 295 O4' - C1' - N1 ANGL. DEV. = 5.8 DEGREES REMARK 500 4 C B 297 O4' - C1' - N1 ANGL. DEV. = 4.5 DEGREES REMARK 500 4 TYR A 31 CB - CG - CD2 ANGL. DEV. = -4.4 DEGREES REMARK 500 5 C B 270 O4' - C1' - N1 ANGL. DEV. = 5.2 DEGREES REMARK 500 5 C B 271 O4' - C1' - N1 ANGL. DEV. = 6.8 DEGREES REMARK 500 REMARK 500 THIS ENTRY HAS 239 ANGLE DEVIATIONS. 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 THR A 3 103.29 54.27 REMARK 500 1 ALA A 6 -162.20 -124.29 REMARK 500 1 LYS A 14 -27.76 144.16 REMARK 500 1 LYS A 34 -28.96 178.13 REMARK 500 1 GLU A 35 -71.42 -89.15 REMARK 500 1 PRO A 37 -168.88 -66.09 REMARK 500 1 LYS A 46 -77.81 -59.43 REMARK 500 1 TYR A 82 -35.33 -145.16 REMARK 500 1 ARG A 93 92.40 -53.94 REMARK 500 2 THR A 3 100.01 55.22 REMARK 500 2 ASN A 5 92.10 -64.58 REMARK 500 2 GLU A 11 10.42 -66.96 REMARK 500 2 LYS A 14 -28.97 157.01 REMARK 500 2 TYR A 31 -168.80 -119.36 REMARK 500 2 ALA A 36 130.31 61.87 REMARK 500 2 PRO A 37 179.22 -54.02 REMARK 500 2 LYS A 46 -80.06 -61.26 REMARK 500 2 TYR A 82 -56.21 -148.02 REMARK 500 2 ARG A 93 93.54 -57.81 REMARK 500 3 THR A 3 104.22 56.70 REMARK 500 3 ALA A 6 -161.50 -125.38 REMARK 500 3 LYS A 10 12.96 -158.56 REMARK 500 3 LYS A 14 -31.91 141.64 REMARK 500 3 ASN A 24 -9.44 136.90 REMARK 500 3 LYS A 34 -41.18 -143.67 REMARK 500 3 ALA A 36 152.68 63.78 REMARK 500 3 LYS A 46 -75.08 -60.02 REMARK 500 3 GLN A 75 -38.67 -131.19 REMARK 500 3 TYR A 82 -55.20 -147.27 REMARK 500 3 ARG A 93 89.86 -58.09 REMARK 500 4 THR A 3 102.77 58.61 REMARK 500 4 ALA A 6 -161.62 -111.86 REMARK 500 4 LYS A 14 -25.85 135.40 REMARK 500 4 ASN A 24 0.23 136.22 REMARK 500 4 LYS A 34 -26.13 174.59 REMARK 500 4 ALA A 36 163.22 101.66 REMARK 500 4 LYS A 46 -77.65 -58.72 REMARK 500 4 TYR A 82 11.19 -147.56 REMARK 500 4 PRO A 84 49.13 -78.55 REMARK 500 4 HIS A 88 163.78 178.86 REMARK 500 4 ARG A 93 93.45 -58.16 REMARK 500 5 PHE A 2 -78.90 58.97 REMARK 500 5 THR A 3 95.86 62.73 REMARK 500 5 ALA A 6 -161.37 -125.24 REMARK 500 5 LYS A 14 -33.58 140.54 REMARK 500 5 ALA A 23 -85.51 -93.49 REMARK 500 5 ASN A 24 3.63 -176.08 REMARK 500 5 ALA A 36 153.42 61.90 REMARK 500 5 LYS A 46 -73.79 -62.73 REMARK 500 5 ASP A 76 116.35 -160.72 REMARK 500 REMARK 500 THIS ENTRY HAS 209 RAMACHANDRAN OUTLIERS. 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 A B 273 0.06 SIDE CHAIN REMARK 500 1 G B 275 0.09 SIDE CHAIN REMARK 500 1 G B 276 0.11 SIDE CHAIN REMARK 500 1 U B 284 0.07 SIDE CHAIN REMARK 500 1 A B 299 0.07 SIDE CHAIN REMARK 500 1 G B 306 0.09 SIDE CHAIN REMARK 500 2 G B 268 0.07 SIDE CHAIN REMARK 500 2 A B 269 0.06 SIDE CHAIN REMARK 500 2 A B 273 0.09 SIDE CHAIN REMARK 500 2 G B 275 0.13 SIDE CHAIN REMARK 500 2 G B 276 0.07 SIDE CHAIN REMARK 500 2 U B 282 0.06 SIDE CHAIN REMARK 500 2 U B 284 0.06 SIDE CHAIN REMARK 500 2 C B 291 0.07 SIDE CHAIN REMARK 500 2 G B 292 0.07 SIDE CHAIN REMARK 500 2 G B 293 0.09 SIDE CHAIN REMARK 500 2 A B 294 0.08 SIDE CHAIN REMARK 500 2 A B 299 0.07 SIDE CHAIN REMARK 500 2 G B 306 0.07 SIDE CHAIN REMARK 500 2 PHE A 26 0.11 SIDE CHAIN REMARK 500 3 G B 268 0.06 SIDE CHAIN REMARK 500 3 A B 269 0.06 SIDE CHAIN REMARK 500 3 A B 273 0.08 SIDE CHAIN REMARK 500 3 G B 275 0.09 SIDE CHAIN REMARK 500 3 G B 276 0.07 SIDE CHAIN REMARK 500 3 U B 284 0.06 SIDE CHAIN REMARK 500 3 G B 292 0.07 SIDE CHAIN REMARK 500 3 C B 297 0.08 SIDE CHAIN REMARK 500 3 G B 298 0.06 SIDE CHAIN REMARK 500 3 A B 299 0.06 SIDE CHAIN REMARK 500 3 G B 306 0.08 SIDE CHAIN REMARK 500 3 PHE A 26 0.10 SIDE CHAIN REMARK 500 4 A B 273 0.10 SIDE CHAIN REMARK 500 4 G B 275 0.13 SIDE CHAIN REMARK 500 4 G B 276 0.05 SIDE CHAIN REMARK 500 4 U B 284 0.10 SIDE CHAIN REMARK 500 4 PHE A 26 0.09 SIDE CHAIN REMARK 500 5 G B 268 0.06 SIDE CHAIN REMARK 500 5 A B 273 0.10 SIDE CHAIN REMARK 500 5 G B 275 0.10 SIDE CHAIN REMARK 500 5 U B 282 0.07 SIDE CHAIN REMARK 500 5 C B 291 0.07 SIDE CHAIN REMARK 500 5 G B 293 0.10 SIDE CHAIN REMARK 500 5 G B 296 0.07 SIDE CHAIN REMARK 500 5 A B 299 0.09 SIDE CHAIN REMARK 500 5 G B 306 0.09 SIDE CHAIN REMARK 500 5 U B 307 0.09 SIDE CHAIN REMARK 500 5 PHE A 26 0.09 SIDE CHAIN REMARK 500 6 A B 273 0.05 SIDE CHAIN REMARK 500 6 G B 275 0.07 SIDE CHAIN REMARK 500 REMARK 500 THIS ENTRY HAS 207 PLANE DEVIATIONS. REMARK 500 REMARK 500 REMARK: NULL DBREF 1D6K A 1 94 UNP P68919 RL25_ECOLI 1 94 DBREF 1D6K B 267 308 PDB 1D6K 1D6K 267 308 SEQRES 1 B 37 G G A C C G A U G G U A G SEQRES 2 B 37 U G U C U U C G G A U G C SEQRES 3 B 37 G A G A G U A G G U C SEQRES 1 A 94 MET PHE THR ILE ASN ALA GLU VAL ARG LYS GLU GLN GLY SEQRES 2 A 94 LYS GLY ALA SER ARG ARG LEU ARG ALA ALA ASN LYS PHE SEQRES 3 A 94 PRO ALA ILE ILE TYR GLY GLY LYS GLU ALA PRO LEU ALA SEQRES 4 A 94 ILE GLU LEU ASP HIS ASP LYS VAL MET ASN MET GLN ALA SEQRES 5 A 94 LYS ALA GLU PHE TYR SER GLU VAL LEU THR ILE VAL VAL SEQRES 6 A 94 ASP GLY LYS GLU ILE LYS VAL LYS ALA GLN ASP VAL GLN SEQRES 7 A 94 ARG HIS PRO TYR LYS PRO LYS LEU GLN HIS ILE ASP PHE SEQRES 8 A 94 VAL ARG ALA HELIX 1 1 LYS A 14 ARG A 21 1 8 HELIX 2 2 HIS A 44 ALA A 52 1 9 HELIX 3 3 ALA A 54 GLU A 59 1 6 SHEET 1 A 7 ALA A 6 VAL A 8 0 SHEET 2 A 7 LEU A 38 ASP A 43 -1 N GLU A 41 O GLU A 7 SHEET 3 A 7 LYS A 25 TYR A 31 -1 N PHE A 26 O LEU A 42 SHEET 4 A 7 LEU A 86 ARG A 93 1 O ILE A 89 N ILE A 29 SHEET 5 A 7 LYS A 68 ARG A 79 -1 O LYS A 73 N VAL A 92 SHEET 6 A 7 LEU A 61 VAL A 65 -1 N LEU A 61 O VAL A 72 SHEET 7 A 7 ALA A 6 VAL A 8 1 N ALA A 6 O VAL A 64 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 23 2 Bytes