Header list of 1zyi.pdb file
Complete list - r 2 2 Bytes
HEADER TRANSLATION 10-JUN-05 1ZYI TITLE SOLUTION STRUCTURE OF ICLN, A MULTIFUNCTIONAL PROTEIN INVOLVED IN TITLE 2 REGULATORY MECHANISMS AS DIFFERENT AS CELL VOLUME REGULATION AND RNA TITLE 3 SPLICING COMPND MOL_ID: 1; COMPND 2 MOLECULE: METHYLOSOME SUBUNIT PICLN; COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: RESIDUES 18 - 133; COMPND 5 SYNONYM: CHLORIDE CONDUCTANCE REGULATORY PROTEIN ICLN; I(CLN); COMPND 6 CHLORIDE CHANNEL, NUCLEOTIDE SENSITIVE 1A; COMPND 7 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: CANIS LUPUS FAMILIARIS; SOURCE 3 ORGANISM_COMMON: DOG; SOURCE 4 ORGANISM_TAXID: 9615; SOURCE 5 STRAIN: FAMILIARIS; SOURCE 6 GENE: CLNS1A, ICLN; SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3); SOURCE 8 EXPRESSION_SYSTEM_TAXID: 469008; SOURCE 9 EXPRESSION_SYSTEM_STRAIN: BL21(DE3); SOURCE 10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 11 EXPRESSION_SYSTEM_PLASMID: PET3-HIS KEYWDS PH DOMAIN; ICLN; CELL VOLUME REGULATION; RNA SPLICING, TRANSLATION EXPDTA SOLUTION NMR NUMMDL 15 AUTHOR J.FUERST,A.SCHEDLBAUER,R.GANDINI,M.L.GARAVAGLIA,S.SIANO, AUTHOR 2 M.GSCHWENTNER,B.SARG,G.KONTAXIS,R.KONRAT,M.PAULMICHL REVDAT 4 02-MAR-22 1ZYI 1 REMARK SEQADV REVDAT 3 24-FEB-09 1ZYI 1 VERSN REVDAT 2 13-DEC-05 1ZYI 1 JRNL REVDAT 1 28-JUN-05 1ZYI 0 JRNL AUTH A.SCHEDLBAUER,R.GANDINI,M.L.GARAVAGLIA,S.SAINO, JRNL AUTH 2 M.GSCHWENTNER,B.SARG,H.LINDNER,M.JAKAB,M.RITTER,C.BAZZINI, JRNL AUTH 3 G.BOTTA,G.MEYER,G.KONTAXIS,B.C.TILLY,R.KONRAT,M.PAULMICHL JRNL TITL ICLN159 FOLDS INTO A PLECKSTRIN HOMOLOGY DOMAIN-LIKE JRNL TITL 2 STRUCTURE. INTERACTION WITH KINASES AND THE SPLICING FACTOR JRNL TITL 3 LSM4 JRNL REF J.BIOL.CHEM. V. 280 31276 2005 JRNL REFN ISSN 0021-9258 JRNL PMID 15905169 JRNL DOI 10.1074/JBC.M500541200 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : X-PLOR-NIH 2.11 REMARK 3 AUTHORS : SCHWIETERS, C.D., KUSZEWSKI, J.J., TJANDRA, N., REMARK 3 CLORE, M., REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 1ZYI COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 17-JUN-05. REMARK 100 THE DEPOSITION ID IS D_1000033269. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 298 REMARK 210 PH : 7.0 REMARK 210 IONIC STRENGTH : 25MM POTASSIUM PHOSPHATE, 150MM REMARK 210 NACL. REMARK 210 PRESSURE : AMBIENT REMARK 210 SAMPLE CONTENTS : 1MM ICLN, 150MM NACL, 25MM REMARK 210 PHOSPHATE BUFFER. REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_13C-SEPARATED_NOESY; 3D_15N REMARK 210 -SEPARATED_NOESY; 3D_CCH-TOCSY- REMARK 210 NNH; 3D_HCCH-TOCSY-NNH; 3D_TOCSY- REMARK 210 HSQC REMARK 210 SPECTROMETER FIELD STRENGTH : 800 MHZ; 500 MHZ REMARK 210 SPECTROMETER MODEL : INOVA REMARK 210 SPECTROMETER MANUFACTURER : VARIAN REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : NULL REMARK 210 METHOD USED : SIMULATED ANNEALING REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 120 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 15 REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LEAST REMARK 210 RESTRAINT VIOLATIONS AND REMARK 210 STRUCTURES WITH THE LOWEST ENERGY REMARK 210 REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL 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 1-15 REMARK 465 RES C SSSEQI REMARK 465 MET A 1 REMARK 465 HIS A 2 REMARK 465 HIS A 3 REMARK 465 HIS A 4 REMARK 465 HIS A 5 REMARK 465 HIS A 6 REMARK 465 HIS A 7 REMARK 465 LEU A 8 REMARK 465 GLU A 9 REMARK 465 MET A 10 REMARK 465 SER A 11 REMARK 465 PHE A 12 REMARK 465 LEU A 13 REMARK 465 LYS A 14 REMARK 465 SER A 15 REMARK 465 PHE A 16 REMARK 465 PRO A 17 REMARK 465 PRO A 18 REMARK 465 PRO A 19 REMARK 465 GLY A 20 REMARK 465 SER A 21 REMARK 465 ALA A 22 REMARK 465 GLU A 23 REMARK 465 GLY A 24 REMARK 465 LEU A 25 REMARK 465 ARG A 26 REMARK 465 HIS A 143 REMARK 465 PRO A 144 REMARK 465 ASP A 145 REMARK 465 PRO A 146 REMARK 465 GLU A 147 REMARK 465 ASP A 148 REMARK 465 GLU A 149 REMARK 465 ASP A 150 REMARK 465 SER A 151 REMARK 465 ASP A 152 REMARK 465 ASP A 153 REMARK 465 TYR A 154 REMARK 465 ASP A 155 REMARK 465 GLY A 156 REMARK 465 GLU A 157 REMARK 465 GLU A 158 REMARK 465 TYR A 159 REMARK 465 ASP A 160 REMARK 465 VAL A 161 REMARK 465 GLU A 162 REMARK 465 ALA A 163 REMARK 465 HIS A 164 REMARK 465 GLU A 165 REMARK 465 GLN A 166 REMARK 465 GLY A 167 REMARK 465 GLN A 168 REMARK 465 GLU A 169 REMARK 465 ASN A 170 REMARK 465 ASP A 171 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: 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 PRO A 30 -82.24 -78.15 REMARK 500 1 ASN A 37 17.57 58.06 REMARK 500 1 ARG A 52 -178.24 -174.33 REMARK 500 1 TYR A 67 141.73 62.27 REMARK 500 1 SER A 71 -73.64 -126.13 REMARK 500 1 ASN A 80 -53.35 -155.18 REMARK 500 1 HIS A 86 131.88 -173.21 REMARK 500 1 GLU A 97 -86.32 56.36 REMARK 500 1 LYS A 100 -41.21 -133.05 REMARK 500 2 SER A 51 25.33 -141.20 REMARK 500 2 GLU A 66 95.39 -69.62 REMARK 500 2 TYR A 67 170.51 57.25 REMARK 500 2 THR A 69 59.19 -101.36 REMARK 500 2 SER A 71 -74.75 -112.01 REMARK 500 2 ASN A 80 27.07 -140.41 REMARK 500 2 ALA A 81 -72.21 -156.28 REMARK 500 2 ALA A 104 -49.82 -132.38 REMARK 500 2 ASP A 112 46.35 -92.34 REMARK 500 3 THR A 69 46.85 -93.55 REMARK 500 3 SER A 71 -72.16 -131.95 REMARK 500 3 ASN A 80 -53.11 -149.96 REMARK 500 3 LYS A 100 70.64 53.62 REMARK 500 3 ALA A 104 -64.47 -94.31 REMARK 500 3 GLU A 105 -45.50 -139.86 REMARK 500 3 GLU A 106 177.84 53.30 REMARK 500 3 ASP A 110 -87.39 55.27 REMARK 500 3 PRO A 115 -84.16 -73.12 REMARK 500 4 PRO A 30 -91.06 -72.81 REMARK 500 4 SER A 71 -68.41 -126.03 REMARK 500 4 ARG A 77 -63.57 -95.40 REMARK 500 4 LEU A 79 119.90 -170.84 REMARK 500 4 ASN A 80 32.73 -168.72 REMARK 500 4 ALA A 81 -45.39 -160.33 REMARK 500 4 HIS A 86 135.10 -170.08 REMARK 500 4 VAL A 103 76.22 53.69 REMARK 500 4 GLU A 105 -56.78 -151.51 REMARK 500 4 ASP A 110 32.37 -168.78 REMARK 500 4 ASP A 111 -72.05 -94.63 REMARK 500 4 SER A 124 31.08 -99.94 REMARK 500 5 PRO A 30 -79.17 -84.71 REMARK 500 5 GLU A 50 103.60 -57.35 REMARK 500 5 GLU A 66 31.04 -153.39 REMARK 500 5 SER A 71 -78.62 -125.35 REMARK 500 5 VAL A 75 -41.29 -159.90 REMARK 500 5 SER A 76 77.36 -67.68 REMARK 500 5 ASN A 80 -45.65 -161.64 REMARK 500 6 PRO A 30 -72.88 -84.86 REMARK 500 6 GLU A 50 103.41 -52.97 REMARK 500 6 SER A 71 -72.28 -109.82 REMARK 500 6 ASN A 80 -40.29 -170.58 REMARK 500 REMARK 500 THIS ENTRY HAS 145 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 ARG A 52 0.26 SIDE CHAIN REMARK 500 1 ARG A 77 0.27 SIDE CHAIN REMARK 500 1 ARG A 84 0.26 SIDE CHAIN REMARK 500 1 ARG A 120 0.27 SIDE CHAIN REMARK 500 2 ARG A 52 0.31 SIDE CHAIN REMARK 500 2 ARG A 77 0.27 SIDE CHAIN REMARK 500 2 ARG A 84 0.29 SIDE CHAIN REMARK 500 2 ARG A 120 0.28 SIDE CHAIN REMARK 500 3 ARG A 52 0.29 SIDE CHAIN REMARK 500 3 ARG A 77 0.24 SIDE CHAIN REMARK 500 3 ARG A 84 0.30 SIDE CHAIN REMARK 500 3 ARG A 120 0.28 SIDE CHAIN REMARK 500 4 ARG A 52 0.27 SIDE CHAIN REMARK 500 4 ARG A 77 0.31 SIDE CHAIN REMARK 500 4 ARG A 84 0.32 SIDE CHAIN REMARK 500 4 ARG A 120 0.28 SIDE CHAIN REMARK 500 5 ARG A 52 0.21 SIDE CHAIN REMARK 500 5 ARG A 77 0.30 SIDE CHAIN REMARK 500 5 ARG A 84 0.26 SIDE CHAIN REMARK 500 5 ARG A 120 0.24 SIDE CHAIN REMARK 500 6 ARG A 52 0.27 SIDE CHAIN REMARK 500 6 ARG A 77 0.29 SIDE CHAIN REMARK 500 6 ARG A 84 0.31 SIDE CHAIN REMARK 500 6 ARG A 120 0.23 SIDE CHAIN REMARK 500 7 ARG A 52 0.31 SIDE CHAIN REMARK 500 7 ARG A 77 0.27 SIDE CHAIN REMARK 500 7 ARG A 84 0.23 SIDE CHAIN REMARK 500 7 ARG A 120 0.23 SIDE CHAIN REMARK 500 8 ARG A 52 0.30 SIDE CHAIN REMARK 500 8 ARG A 77 0.31 SIDE CHAIN REMARK 500 8 ARG A 84 0.27 SIDE CHAIN REMARK 500 8 ARG A 120 0.32 SIDE CHAIN REMARK 500 9 ARG A 52 0.21 SIDE CHAIN REMARK 500 9 ARG A 77 0.31 SIDE CHAIN REMARK 500 9 ARG A 84 0.31 SIDE CHAIN REMARK 500 9 ARG A 120 0.31 SIDE CHAIN REMARK 500 10 ARG A 52 0.32 SIDE CHAIN REMARK 500 10 ARG A 77 0.25 SIDE CHAIN REMARK 500 10 ARG A 84 0.27 SIDE CHAIN REMARK 500 10 ARG A 120 0.28 SIDE CHAIN REMARK 500 11 ARG A 52 0.26 SIDE CHAIN REMARK 500 11 ARG A 77 0.30 SIDE CHAIN REMARK 500 11 ARG A 84 0.31 SIDE CHAIN REMARK 500 11 ARG A 120 0.18 SIDE CHAIN REMARK 500 12 ARG A 52 0.26 SIDE CHAIN REMARK 500 12 ARG A 77 0.26 SIDE CHAIN REMARK 500 12 ARG A 84 0.32 SIDE CHAIN REMARK 500 12 ARG A 120 0.31 SIDE CHAIN REMARK 500 13 ARG A 52 0.32 SIDE CHAIN REMARK 500 13 ARG A 77 0.32 SIDE CHAIN REMARK 500 REMARK 500 THIS ENTRY HAS 60 PLANE DEVIATIONS. REMARK 500 REMARK 500 REMARK: NULL DBREF 1ZYI A 27 142 UNP P35521 ICLN_CANFA 18 133 SEQADV 1ZYI MET A 1 UNP P35521 EXPRESSION TAG SEQADV 1ZYI HIS A 2 UNP P35521 EXPRESSION TAG SEQADV 1ZYI HIS A 3 UNP P35521 EXPRESSION TAG SEQADV 1ZYI HIS A 4 UNP P35521 EXPRESSION TAG SEQADV 1ZYI HIS A 5 UNP P35521 EXPRESSION TAG SEQADV 1ZYI HIS A 6 UNP P35521 EXPRESSION TAG SEQADV 1ZYI HIS A 7 UNP P35521 EXPRESSION TAG SEQADV 1ZYI LEU A 8 UNP P35521 EXPRESSION TAG SEQADV 1ZYI GLU A 9 UNP P35521 EXPRESSION TAG SEQADV 1ZYI MET A 10 UNP P35521 EXPRESSION TAG SEQADV 1ZYI SER A 11 UNP P35521 EXPRESSION TAG SEQADV 1ZYI PHE A 12 UNP P35521 EXPRESSION TAG SEQADV 1ZYI LEU A 13 UNP P35521 EXPRESSION TAG SEQADV 1ZYI LYS A 14 UNP P35521 EXPRESSION TAG SEQADV 1ZYI SER A 15 UNP P35521 EXPRESSION TAG SEQADV 1ZYI PHE A 16 UNP P35521 EXPRESSION TAG SEQADV 1ZYI PRO A 17 UNP P35521 EXPRESSION TAG SEQADV 1ZYI PRO A 18 UNP P35521 EXPRESSION TAG SEQADV 1ZYI PRO A 19 UNP P35521 EXPRESSION TAG SEQADV 1ZYI GLY A 20 UNP P35521 EXPRESSION TAG SEQADV 1ZYI SER A 21 UNP P35521 EXPRESSION TAG SEQADV 1ZYI ALA A 22 UNP P35521 EXPRESSION TAG SEQADV 1ZYI GLU A 23 UNP P35521 EXPRESSION TAG SEQADV 1ZYI GLY A 24 UNP P35521 EXPRESSION TAG SEQADV 1ZYI LEU A 25 UNP P35521 EXPRESSION TAG SEQADV 1ZYI ARG A 26 UNP P35521 EXPRESSION TAG SEQADV 1ZYI HIS A 143 UNP P35521 CLONING ARTIFACT SEQADV 1ZYI PRO A 144 UNP P35521 CLONING ARTIFACT SEQADV 1ZYI ASP A 145 UNP P35521 CLONING ARTIFACT SEQADV 1ZYI PRO A 146 UNP P35521 CLONING ARTIFACT SEQADV 1ZYI GLU A 147 UNP P35521 CLONING ARTIFACT SEQADV 1ZYI ASP A 148 UNP P35521 CLONING ARTIFACT SEQADV 1ZYI GLU A 149 UNP P35521 CLONING ARTIFACT SEQADV 1ZYI ASP A 150 UNP P35521 CLONING ARTIFACT SEQADV 1ZYI SER A 151 UNP P35521 CLONING ARTIFACT SEQADV 1ZYI ASP A 152 UNP P35521 CLONING ARTIFACT SEQADV 1ZYI ASP A 153 UNP P35521 CLONING ARTIFACT SEQADV 1ZYI TYR A 154 UNP P35521 CLONING ARTIFACT SEQADV 1ZYI ASP A 155 UNP P35521 CLONING ARTIFACT SEQADV 1ZYI GLY A 156 UNP P35521 CLONING ARTIFACT SEQADV 1ZYI GLU A 157 UNP P35521 CLONING ARTIFACT SEQADV 1ZYI GLU A 158 UNP P35521 CLONING ARTIFACT SEQADV 1ZYI TYR A 159 UNP P35521 CLONING ARTIFACT SEQADV 1ZYI ASP A 160 UNP P35521 CLONING ARTIFACT SEQADV 1ZYI VAL A 161 UNP P35521 CLONING ARTIFACT SEQADV 1ZYI GLU A 162 UNP P35521 CLONING ARTIFACT SEQADV 1ZYI ALA A 163 UNP P35521 CLONING ARTIFACT SEQADV 1ZYI HIS A 164 UNP P35521 CLONING ARTIFACT SEQADV 1ZYI GLU A 165 UNP P35521 CLONING ARTIFACT SEQADV 1ZYI GLN A 166 UNP P35521 CLONING ARTIFACT SEQADV 1ZYI GLY A 167 UNP P35521 CLONING ARTIFACT SEQADV 1ZYI GLN A 168 UNP P35521 CLONING ARTIFACT SEQADV 1ZYI GLU A 169 UNP P35521 CLONING ARTIFACT SEQADV 1ZYI ASN A 170 UNP P35521 CLONING ARTIFACT SEQADV 1ZYI ASP A 171 UNP P35521 CLONING ARTIFACT SEQRES 1 A 171 MET HIS HIS HIS HIS HIS HIS LEU GLU MET SER PHE LEU SEQRES 2 A 171 LYS SER PHE PRO PRO PRO GLY SER ALA GLU GLY LEU ARG SEQRES 3 A 171 GLN GLN GLN PRO GLU THR GLU ALA VAL LEU ASN GLY LYS SEQRES 4 A 171 GLY LEU GLY THR GLY THR LEU TYR ILE ALA GLU SER ARG SEQRES 5 A 171 LEU SER TRP LEU ASP GLY SER GLY LEU GLY PHE SER LEU SEQRES 6 A 171 GLU TYR PRO THR ILE SER LEU HIS ALA VAL SER ARG ASP SEQRES 7 A 171 LEU ASN ALA TYR PRO ARG GLU HIS LEU TYR VAL MET VAL SEQRES 8 A 171 ASN ALA LYS PHE GLY GLU GLU SER LYS GLU SER VAL ALA SEQRES 9 A 171 GLU GLU GLU ASP SER ASP ASP ASP VAL GLU PRO ILE ALA SEQRES 10 A 171 GLU PHE ARG PHE VAL PRO SER ASP LYS SER ALA LEU GLU SEQRES 11 A 171 ALA MET PHE THR ALA MET CYS GLU CYS GLN ALA LEU HIS SEQRES 12 A 171 PRO ASP PRO GLU ASP GLU ASP SER ASP ASP TYR ASP GLY SEQRES 13 A 171 GLU GLU TYR ASP VAL GLU ALA HIS GLU GLN GLY GLN GLU SEQRES 14 A 171 ASN ASP HELIX 1 1 ASP A 125 LEU A 142 1 18 SHEET 1 A 7 LEU A 61 LEU A 65 0 SHEET 2 A 7 ARG A 52 ASP A 57 -1 N TRP A 55 O PHE A 63 SHEET 3 A 7 THR A 43 ALA A 49 -1 N THR A 45 O LEU A 56 SHEET 4 A 7 THR A 32 VAL A 35 -1 N THR A 32 O GLY A 44 SHEET 5 A 7 ILE A 116 PRO A 123 -1 O ARG A 120 N VAL A 35 SHEET 6 A 7 LEU A 87 ASN A 92 -1 N LEU A 87 O PHE A 121 SHEET 7 A 7 LEU A 72 ALA A 74 -1 N ALA A 74 O TYR A 88 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