Header list of 1ykg.pdb file
Complete list - r 2 2 Bytes
HEADER ELECTRON TRANSPORT 18-JAN-05 1YKG TITLE SOLUTION STRUCTURE OF THE FLAVODOXIN-LIKE DOMAIN FROM THE ESCHERICHIA TITLE 2 COLI SULFITE REDUCTASE COMPND MOL_ID: 1; COMPND 2 MOLECULE: SULFITE REDUCTASE [NADPH] FLAVOPROTEIN ALPHA-COMPONENT; COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: SIR-FP18, FLAVODOXIN-LIKE DOMAIN; COMPND 5 SYNONYM: SIR-FP; COMPND 6 EC: 1.8.1.2; COMPND 7 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI; SOURCE 3 ORGANISM_TAXID: 562; SOURCE 4 GENE: CYSJ; SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PET30 KEYWDS FLAVOPROTEIN, ELECTRON TRANSPORT EXPDTA SOLUTION NMR NUMMDL 15 AUTHOR N.SIBILLE,M.BLACKLEDGE,B.BRUTSCHER,J.COVES,B.BERSCH REVDAT 4 02-MAR-22 1YKG 1 REMARK REVDAT 3 21-APR-09 1YKG 1 REMARK REVDAT 2 24-FEB-09 1YKG 1 VERSN REVDAT 1 05-JUL-05 1YKG 0 JRNL AUTH N.SIBILLE,M.BLACKLEDGE,B.BRUTSCHER,J.COVES,B.BERSCH JRNL TITL SOLUTION STRUCTURE OF THE SULFITE REDUCTASE FLAVODOXIN-LIKE JRNL TITL 2 DOMAIN FROM ESCHERICHIA COLI JRNL REF BIOCHEMISTRY V. 44 9086 2005 JRNL REFN ISSN 0006-2960 JRNL PMID 15966732 JRNL DOI 10.1021/BI050437P REMARK 1 REMARK 1 REFERENCE 1 REMARK 1 AUTH L.CHAMPIER,N.SIBILLE,B.BERSCH,B.BRUTSCHER,M.BLACKLEDGE, REMARK 1 AUTH 2 J.COVES REMARK 1 TITL REACTIVITY, SECONDARY STRUCTURE, AND MOLECULAR TOPOLOGY OF REMARK 1 TITL 2 THE ESCHERICHIA COLI SULFITE REDUCTASE FLAVODOXIN-LIKE REMARK 1 TITL 3 DOMAIN REMARK 1 REF BIOCHEMISTRY V. 41 3770 2002 REMARK 1 REFN ISSN 0006-2960 REMARK 1 PMID 11888295 REMARK 1 DOI 10.1021/BI016008I REMARK 1 REFERENCE 2 REMARK 1 AUTH N.SIBILLE,J.COVES,D.MARION,B.BRUTSCHER,B.BERSCH REMARK 1 TITL 1H, 13C, AND 15N ASSIGNMENT OF THE FLAVODOXIN-LIKE DOMAIN OF REMARK 1 TITL 2 THE ESCHERICHIA COLI SULFITE REDUCTASE REMARK 1 REF J.BIOMOL.NMR V. 21 71 2001 REMARK 1 REFN ISSN 0925-2738 REMARK 1 PMID 11693572 REMARK 1 DOI 10.1023/A:1011985803535 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : DISCOVER 2.98, SCULPTOR 1 REMARK 3 AUTHORS : ACCELRYS INC. (DISCOVER), HUS, J.C., BLACKLEDGE, REMARK 3 M. (SCULPTOR) REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: RESIDUES 52-62 AND 209-218 ARE REMARK 3 DISORDERED AND ARE NOT INCLUDED IN THE PDB FILE. REMARK 4 REMARK 4 1YKG COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 21-JAN-05. REMARK 100 THE DEPOSITION ID IS D_1000031616. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 303; 303 REMARK 210 PH : 7; 7 REMARK 210 IONIC STRENGTH : 100MM PHOSPHATE BUFFER; 100MM REMARK 210 PHOSPHATE BUFFER, 2MM MGCL2 REMARK 210 PRESSURE : AMBIENT; AMBIENT REMARK 210 SAMPLE CONTENTS : 1.5MM U-15N, U-13C, 80%-2H SIR REMARK 210 -FP18; 1.5MM U-15N, U-13C, SIR- REMARK 210 FP18; 1.5MM U-15N, U-13C, SIR- REMARK 210 FP18; 1.5MM U-15N, SIR-FP18; REMARK 210 1.5MM U-15N, U-13C, 80%-2H SIR- REMARK 210 FP18; 1.5MM U-15N, U-13C, 80%-2H REMARK 210 SIR-FP18; 1.5MM U-15N, SIR-FP18 REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY; 3D_13C REMARK 210 -SEPARATED_NOESY; 2D NOESY REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ; 800 MHZ REMARK 210 SPECTROMETER MODEL : INOVA REMARK 210 SPECTROMETER MANUFACTURER : VARIAN REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : FELIX 2000 REMARK 210 METHOD USED : SIMULATED ANNEALING REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 15 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 15 REMARK 210 CONFORMERS, SELECTION CRITERIA : INITIAL SELECTION BASED ON REMARK 210 EXPERIMENTAL ENERGY TARGET REMARK 210 FUNCTION REMARK 210 REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 2 REMARK 210 REMARK 210 REMARK: RESIDUAL DIPOLAR COUPLINGS AND 3HJNC COUPLINGS FOR THE REMARK 210 DETECTION OF HYDROGEN-BONDS HAVE BEEN MEASURED USING 3D-HNCO- REMARK 210 TYPE EXPERIMENTS. 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 ALA A 52 REMARK 465 THR A 53 REMARK 465 PRO A 54 REMARK 465 ALA A 55 REMARK 465 PRO A 56 REMARK 465 ALA A 57 REMARK 465 ALA A 58 REMARK 465 GLU A 59 REMARK 465 MET A 60 REMARK 465 PRO A 61 REMARK 465 GLY A 62 REMARK 465 PRO A 209 REMARK 465 VAL A 210 REMARK 465 ALA A 211 REMARK 465 ALA A 212 REMARK 465 PRO A 213 REMARK 465 SER A 214 REMARK 465 GLN A 215 REMARK 465 SER A 216 REMARK 465 VAL A 217 REMARK 465 ALA A 218 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 O GLU A 188 H GLN A 190 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 4 GLU A 126 C - N - CA ANGL. DEV. = 17.6 DEGREES REMARK 500 5 LYS A 138 N - CA - C ANGL. DEV. = -20.0 DEGREES REMARK 500 9 TYR A 100 CB - CG - CD2 ANGL. DEV. = -4.0 DEGREES REMARK 500 11 TYR A 100 CB - CG - CD2 ANGL. DEV. = -4.1 DEGREES REMARK 500 12 PRO A 140 C - N - CA ANGL. DEV. = 9.8 DEGREES REMARK 500 13 LYS A 138 N - CA - C ANGL. DEV. = -17.4 DEGREES REMARK 500 13 ARG A 182 NE - CZ - NH2 ANGL. DEV. = -3.5 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 LYS A 89 -69.06 -146.11 REMARK 500 1 LEU A 90 -53.73 131.83 REMARK 500 1 PHE A 102 -1.64 -56.02 REMARK 500 1 ASN A 144 46.40 -152.26 REMARK 500 1 TYR A 189 -47.55 40.48 REMARK 500 2 GLU A 120 -67.57 70.99 REMARK 500 2 ASN A 144 33.67 -148.54 REMARK 500 2 GLU A 188 47.52 -80.05 REMARK 500 3 LYS A 89 38.85 70.37 REMARK 500 3 LEU A 142 50.58 -97.75 REMARK 500 3 ASN A 144 67.28 -152.60 REMARK 500 3 GLU A 188 47.94 -79.98 REMARK 500 4 LYS A 89 38.18 72.23 REMARK 500 4 PHE A 102 -1.11 -54.54 REMARK 500 4 GLU A 125 -73.04 -56.16 REMARK 500 4 GLU A 126 -1.79 -39.41 REMARK 500 4 SER A 136 -178.81 -173.34 REMARK 500 4 ASN A 144 39.79 -148.07 REMARK 500 4 TYR A 189 -43.30 34.31 REMARK 500 5 PHE A 102 -6.20 -59.18 REMARK 500 5 ALA A 106 6.04 -65.46 REMARK 500 5 ALA A 139 78.64 175.61 REMARK 500 5 LEU A 142 49.26 -82.11 REMARK 500 5 CYS A 161 40.55 -145.40 REMARK 500 5 GLU A 188 47.86 -80.06 REMARK 500 6 LEU A 142 42.91 -87.49 REMARK 500 6 TYR A 189 -44.89 35.11 REMARK 500 7 LYS A 89 39.13 70.27 REMARK 500 7 ALA A 106 7.90 -60.22 REMARK 500 7 PHE A 135 -105.86 -74.27 REMARK 500 7 SER A 136 123.59 -3.16 REMARK 500 7 LYS A 137 1.73 -51.32 REMARK 500 7 ASN A 144 63.62 -160.55 REMARK 500 7 GLU A 188 48.95 -81.96 REMARK 500 8 ALA A 106 0.95 -59.84 REMARK 500 8 PHE A 135 -95.25 -91.60 REMARK 500 8 LYS A 137 15.67 -51.99 REMARK 500 8 LYS A 138 47.60 81.81 REMARK 500 8 LEU A 142 36.34 -97.43 REMARK 500 8 ARG A 207 40.46 -142.55 REMARK 500 9 LYS A 89 32.36 70.95 REMARK 500 9 ALA A 106 3.01 -58.79 REMARK 500 9 ASN A 144 41.94 -151.67 REMARK 500 9 GLU A 188 48.16 -78.07 REMARK 500 9 ARG A 207 33.50 -142.27 REMARK 500 10 LYS A 89 36.16 70.11 REMARK 500 10 PHE A 135 -90.43 -82.32 REMARK 500 10 SER A 136 119.28 -3.01 REMARK 500 10 LYS A 138 1.98 -64.81 REMARK 500 10 LYS A 141 -139.38 52.93 REMARK 500 REMARK 500 THIS ENTRY HAS 84 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 TYR A 100 0.07 SIDE CHAIN REMARK 500 1 PHE A 147 0.09 SIDE CHAIN REMARK 500 1 TYR A 157 0.12 SIDE CHAIN REMARK 500 2 PHE A 102 0.11 SIDE CHAIN REMARK 500 3 PHE A 102 0.09 SIDE CHAIN REMARK 500 3 TYR A 157 0.11 SIDE CHAIN REMARK 500 3 TYR A 189 0.08 SIDE CHAIN REMARK 500 4 TYR A 157 0.13 SIDE CHAIN REMARK 500 4 ARG A 197 0.08 SIDE CHAIN REMARK 500 6 PHE A 102 0.10 SIDE CHAIN REMARK 500 7 PHE A 102 0.11 SIDE CHAIN REMARK 500 7 TYR A 157 0.13 SIDE CHAIN REMARK 500 7 TYR A 189 0.10 SIDE CHAIN REMARK 500 8 PHE A 102 0.09 SIDE CHAIN REMARK 500 8 TYR A 157 0.08 SIDE CHAIN REMARK 500 9 PHE A 102 0.10 SIDE CHAIN REMARK 500 9 TYR A 157 0.11 SIDE CHAIN REMARK 500 10 PHE A 102 0.14 SIDE CHAIN REMARK 500 10 TYR A 157 0.09 SIDE CHAIN REMARK 500 11 ARG A 75 0.10 SIDE CHAIN REMARK 500 11 PHE A 102 0.10 SIDE CHAIN REMARK 500 12 PHE A 102 0.12 SIDE CHAIN REMARK 500 12 TYR A 157 0.16 SIDE CHAIN REMARK 500 12 ARG A 178 0.08 SIDE CHAIN REMARK 500 12 TYR A 189 0.11 SIDE CHAIN REMARK 500 13 PHE A 102 0.12 SIDE CHAIN REMARK 500 13 TYR A 157 0.07 SIDE CHAIN REMARK 500 14 PHE A 102 0.11 SIDE CHAIN REMARK 500 14 TYR A 157 0.10 SIDE CHAIN REMARK 500 15 PHE A 102 0.13 SIDE CHAIN REMARK 500 15 TYR A 157 0.09 SIDE CHAIN REMARK 500 15 ARG A 182 0.08 SIDE CHAIN REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY REMARK 500 REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME; REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; REMARK 500 I=INSERTION CODE). REMARK 500 REMARK 500 M RES CSSEQI ANGLE REMARK 500 1 THR A 71 -13.95 REMARK 500 1 GLU A 188 -12.27 REMARK 500 2 THR A 71 -12.10 REMARK 500 3 THR A 71 -13.42 REMARK 500 4 THR A 71 -13.43 REMARK 500 4 GLU A 125 10.14 REMARK 500 4 GLU A 188 -11.73 REMARK 500 5 THR A 71 -11.99 REMARK 500 6 THR A 71 -14.93 REMARK 500 6 GLU A 188 -11.67 REMARK 500 7 THR A 71 -14.00 REMARK 500 8 THR A 71 -14.01 REMARK 500 9 THR A 71 -15.20 REMARK 500 9 GLY A 121 13.18 REMARK 500 10 THR A 71 -14.27 REMARK 500 10 GLU A 188 -11.59 REMARK 500 11 THR A 71 -14.98 REMARK 500 12 THR A 71 -14.58 REMARK 500 13 THR A 71 -14.82 REMARK 500 14 THR A 71 -13.53 REMARK 500 14 GLU A 158 25.89 REMARK 500 15 THR A 71 -13.63 REMARK 500 15 GLY A 121 14.55 REMARK 500 15 LYS A 137 -15.80 REMARK 500 REMARK 500 REMARK: NULL REMARK 800 REMARK 800 SITE REMARK 800 SITE_IDENTIFIER: AC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMN A 300 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 4985 RELATED DB: BMRB DBREF 1YKG A 52 218 UNP P38038 CYSJ_ECOLI 52 218 SEQRES 1 A 167 ALA THR PRO ALA PRO ALA ALA GLU MET PRO GLY ILE THR SEQRES 2 A 167 ILE ILE SER ALA SER GLN THR GLY ASN ALA ARG ARG VAL SEQRES 3 A 167 ALA GLU ALA LEU ARG ASP ASP LEU LEU ALA ALA LYS LEU SEQRES 4 A 167 ASN VAL LYS LEU VAL ASN ALA GLY ASP TYR LYS PHE LYS SEQRES 5 A 167 GLN ILE ALA SER GLU LYS LEU LEU ILE VAL VAL THR SER SEQRES 6 A 167 THR GLN GLY GLU GLY GLU PRO PRO GLU GLU ALA VAL ALA SEQRES 7 A 167 LEU HIS LYS PHE LEU PHE SER LYS LYS ALA PRO LYS LEU SEQRES 8 A 167 GLU ASN THR ALA PHE ALA VAL PHE SER LEU GLY ASP THR SEQRES 9 A 167 SER TYR GLU PHE PHE CYS GLN SER GLY LYS ASP PHE ASP SEQRES 10 A 167 SER LYS LEU ALA GLU LEU GLY GLY GLU ARG LEU LEU ASP SEQRES 11 A 167 ARG VAL ASP ALA ASP VAL GLU TYR GLN ALA ALA ALA SER SEQRES 12 A 167 GLU TRP ARG ALA ARG VAL VAL ASP ALA LEU LYS SER ARG SEQRES 13 A 167 ALA PRO VAL ALA ALA PRO SER GLN SER VAL ALA HET FMN A 300 50 HETNAM FMN FLAVIN MONONUCLEOTIDE HETSYN FMN RIBOFLAVIN MONOPHOSPHATE FORMUL 2 FMN C17 H21 N4 O9 P HELIX 1 1 GLY A 72 LYS A 89 1 18 HELIX 2 2 GLY A 98 TYR A 100 5 3 HELIX 3 3 LYS A 101 GLU A 108 5 8 HELIX 4 4 GLN A 118 GLU A 122 5 5 HELIX 5 5 PRO A 124 GLU A 126 5 3 HELIX 6 6 ALA A 127 PHE A 135 1 9 HELIX 7 7 CYS A 161 GLY A 175 1 15 HELIX 8 8 TYR A 189 SER A 206 1 18 SHEET 1 A 5 LYS A 93 ASN A 96 0 SHEET 2 A 5 THR A 64 ALA A 68 1 N ILE A 65 O LYS A 93 SHEET 3 A 5 LEU A 110 SER A 116 1 O ILE A 112 N THR A 64 SHEET 4 A 5 ALA A 146 LEU A 152 1 O ALA A 148 N VAL A 113 SHEET 5 A 5 GLU A 177 ARG A 178 1 O GLU A 177 N PHE A 147 SHEET 1 B 5 LYS A 93 ASN A 96 0 SHEET 2 B 5 THR A 64 ALA A 68 1 N ILE A 65 O LYS A 93 SHEET 3 B 5 LEU A 110 SER A 116 1 O ILE A 112 N THR A 64 SHEET 4 B 5 ALA A 146 LEU A 152 1 O ALA A 148 N VAL A 113 SHEET 5 B 5 VAL A 183 ALA A 185 1 O VAL A 183 N SER A 151 SITE 1 AC1 17 SER A 69 GLN A 70 THR A 71 GLY A 72 SITE 2 AC1 17 ASN A 73 ALA A 74 SER A 116 THR A 117 SITE 3 AC1 17 GLN A 118 GLY A 119 LEU A 152 GLY A 153 SITE 4 AC1 17 ASP A 154 TYR A 157 PHE A 159 PHE A 160 SITE 5 AC1 17 CYS A 161 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