Header list of 1qch.pdb file
Complete list - 2 20 Bytes
HEADER DNA 05-MAY-99 1QCH TITLE STRUCTURE, DYNAMICS AND HYDRATION OF THE NOGALAMYCIN-D(ATGCAT)2 TITLE 2 COMPLEX DETERMINED BY NMR AND MOLECULAR DYNAMICS SIMULATIONS IN TITLE 3 SOLUTION COMPND MOL_ID: 1; COMPND 2 MOLECULE: 5'-D(*AP*TP*GP*CP*AP*T)-3'; COMPND 3 CHAIN: A, B; COMPND 4 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 SYNTHETIC: YES; SOURCE 3 OTHER_DETAILS: SOLID PHASE SYNTHESIS KEYWDS NOGALAMYCIN, NOGALAMYCIN-DNA COMPLEX, NMR SPECTROSCOPY, ANTHRACYCLINE KEYWDS 2 ANTIBIOTIC, HYDRATION, DNA EXPDTA SOLUTION NMR AUTHOR H.E.L.WILLIAMS,M.S.SEARLE REVDAT 5 02-MAR-22 1QCH 1 JRNL REMARK LINK REVDAT 4 24-FEB-09 1QCH 1 VERSN REVDAT 3 01-APR-03 1QCH 1 JRNL REVDAT 2 10-MAY-02 1QCH 1 SCALE1 SCALE2 SCALE3 REMARK REVDAT 1 02-AUG-99 1QCH 0 JRNL AUTH H.E.WILLIAMS,M.S.SEARLE JRNL TITL STRUCTURE, DYNAMICS AND HYDRATION OF THE JRNL TITL 2 NOGALAMYCIN-D(ATGCAT)2COMPLEX DETERMINED BY NMR AND JRNL TITL 3 MOLECULAR DYNAMICS SIMULATIONS IN SOLUTION. JRNL REF J.MOL.BIOL. V. 290 699 1999 JRNL REFN ISSN 0022-2836 JRNL PMID 10395824 JRNL DOI 10.1006/JMBI.1999.2903 REMARK 1 REMARK 1 REFERENCE 1 REMARK 1 AUTH H.E.WILLIAMS,M.S.SEARLE REMARK 1 TITL STRUCTURE OF THE NOGALAMYCIN-D(ATGCAT)(2) COMPLEX IN REMARK 1 TITL 2 SOLUTION: DNA RECOGNITION AT AN ISOLATED TPG SITE REMARK 1 REF J.CHEM.SOC, PERKIN TRANS.1 V. 1 3 1998 REMARK 1 REFN ISSN 0300-922X REMARK 1 DOI 10.1039/A707093D REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : NULL REMARK 3 AUTHORS : NULL REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: 1NS RESTRAINED MOLECULAR DYNAMICS REMARK 4 REMARK 4 1QCH COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY NDB. REMARK 100 THE DEPOSITION ID IS D_1000009072. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : NULL REMARK 210 PH : NULL REMARK 210 IONIC STRENGTH : NULL REMARK 210 PRESSURE : NULL REMARK 210 SAMPLE CONTENTS : NULL REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : NULL REMARK 210 SPECTROMETER FIELD STRENGTH : NULL REMARK 210 SPECTROMETER MODEL : NULL REMARK 210 SPECTROMETER MANUFACTURER : NULL REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : NULL REMARK 210 METHOD USED : MOLECULAR DYNAMICS REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : NULL REMARK 210 CONFORMERS, NUMBER SUBMITTED : 1 REMARK 210 CONFORMERS, SELECTION CRITERIA : NULL 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: DIMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B 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 OP2 DT B 12 H1 HOH B 908 1.57 REMARK 500 OP2 DC B 10 H1 HOH B 2205 1.57 REMARK 500 OP1 DA A 5 H1 HOH A 973 1.59 REMARK 500 O HOH A 1396 H2 HOH A 1611 1.59 REMARK 500 O HOH A 602 H2 HOH A 772 1.59 REMARK 500 H2 HOH A 1074 O HOH A 1758 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 DA A 1 C4 - C5 - C6 ANGL. DEV. = -3.4 DEGREES REMARK 500 DA A 1 C5 - C6 - N1 ANGL. DEV. = 3.4 DEGREES REMARK 500 DA A 1 N1 - C6 - N6 ANGL. DEV. = -5.7 DEGREES REMARK 500 DC A 4 O4' - C1' - N1 ANGL. DEV. = 4.6 DEGREES REMARK 500 DC A 4 N3 - C2 - O2 ANGL. DEV. = -4.8 DEGREES REMARK 500 DA A 5 O4' - C1' - N9 ANGL. DEV. = 2.6 DEGREES REMARK 500 DA A 5 C4 - C5 - C6 ANGL. DEV. = -3.9 DEGREES REMARK 500 DA A 5 C5 - C6 - N1 ANGL. DEV. = 3.4 DEGREES REMARK 500 DA A 5 N1 - C6 - N6 ANGL. DEV. = -6.5 DEGREES REMARK 500 DT A 6 C6 - C5 - C7 ANGL. DEV. = -3.8 DEGREES REMARK 500 DA B 7 O4' - C1' - N9 ANGL. DEV. = 5.2 DEGREES REMARK 500 DA B 7 C4 - C5 - C6 ANGL. DEV. = -3.9 DEGREES REMARK 500 DA B 7 C5 - C6 - N1 ANGL. DEV. = 3.3 DEGREES REMARK 500 DA B 7 N1 - C6 - N6 ANGL. DEV. = -7.0 DEGREES REMARK 500 DT B 8 O4' - C1' - N1 ANGL. DEV. = 3.0 DEGREES REMARK 500 DT B 8 C6 - C5 - C7 ANGL. DEV. = -3.6 DEGREES REMARK 500 DG B 9 O4' - C1' - N9 ANGL. DEV. = 1.9 DEGREES REMARK 500 DC B 10 O4' - C1' - N1 ANGL. DEV. = 2.9 DEGREES REMARK 500 DA B 11 O4' - C1' - N9 ANGL. DEV. = 1.8 DEGREES REMARK 500 DA B 11 C4 - C5 - C6 ANGL. DEV. = -4.1 DEGREES REMARK 500 DA B 11 C5 - C6 - N1 ANGL. DEV. = 3.2 DEGREES REMARK 500 DA B 11 C6 - C5 - N7 ANGL. DEV. = 4.2 DEGREES REMARK 500 DA B 11 N1 - C6 - N6 ANGL. DEV. = -7.0 DEGREES REMARK 500 DT B 12 O4' - C1' - N1 ANGL. DEV. = 1.9 DEGREES 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 DT A 2 0.11 SIDE CHAIN REMARK 500 DA B 11 0.06 SIDE CHAIN REMARK 500 REMARK 500 REMARK: NULL REMARK 620 REMARK 620 METAL COORDINATION REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE): REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 NA A 21 NA REMARK 620 N RES CSSEQI ATOM REMARK 620 1 DT A 6 O2 REMARK 620 2 HOH A 366 O 81.1 REMARK 620 3 DT B 8 O2 92.8 167.6 REMARK 620 4 HOH B 200 O 161.7 81.4 103.4 REMARK 620 5 HOH B1045 O 90.9 85.1 84.3 82.5 REMARK 620 6 HOH B1153 O 94.7 84.8 106.5 88.8 167.5 REMARK 620 N 1 2 3 4 5 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 NA A 16 NA REMARK 620 N RES CSSEQI ATOM REMARK 620 1 HOH A1143 O REMARK 620 2 HOH A1696 O 105.9 REMARK 620 3 HOH A2229 O 97.0 120.0 REMARK 620 4 HOH B1305 O 88.0 126.0 109.1 REMARK 620 N 1 2 3 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 NA B 20 NA REMARK 620 N RES CSSEQI ATOM REMARK 620 1 HOH A 24 O REMARK 620 2 HOH A 572 O 145.7 REMARK 620 3 HOH A1096 O 90.1 73.8 REMARK 620 4 HOH A1977 O 82.5 121.9 159.4 REMARK 620 5 HOH A2035 O 83.6 79.9 121.7 76.7 REMARK 620 6 HOH B 548 O 115.8 92.5 83.0 82.9 149.8 REMARK 620 N 1 2 3 4 5 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 NA B 15 NA REMARK 620 N RES CSSEQI ATOM REMARK 620 1 HOH A 30 O REMARK 620 2 HOH A 263 O 81.3 REMARK 620 3 HOH B 563 O 92.5 91.1 REMARK 620 4 HOH B1186 O 173.5 99.6 93.8 REMARK 620 5 HOH B1259 O 79.4 158.1 79.5 100.8 REMARK 620 6 HOH B1498 O 94.7 86.3 171.8 79.0 105.5 REMARK 620 N 1 2 3 4 5 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 NA B 17 NA REMARK 620 N RES CSSEQI ATOM REMARK 620 1 HOH A 85 O REMARK 620 2 HOH A 778 O 164.0 REMARK 620 3 HOH A1242 O 109.2 85.8 REMARK 620 4 HOH A1554 O 80.2 108.5 81.1 REMARK 620 5 HOH A1658 O 86.0 82.1 154.7 81.8 REMARK 620 6 HOH B1542 O 84.3 84.5 113.5 161.6 87.3 REMARK 620 N 1 2 3 4 5 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 NA B 23 NA REMARK 620 N RES CSSEQI ATOM REMARK 620 1 HOH A 574 O REMARK 620 2 HOH A 643 O 165.9 REMARK 620 3 HOH A 764 O 112.4 78.4 REMARK 620 4 HOH A 779 O 95.6 94.6 83.4 REMARK 620 5 HOH A 794 O 79.5 90.3 167.9 93.3 REMARK 620 6 HOH A1473 O 83.2 86.3 99.1 177.5 84.3 REMARK 620 N 1 2 3 4 5 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 NA B 22 NA REMARK 620 N RES CSSEQI ATOM REMARK 620 1 HOH A 814 O REMARK 620 2 HOH B 319 O 82.9 REMARK 620 3 HOH B 413 O 170.4 88.4 REMARK 620 4 HOH B 482 O 81.3 163.5 106.9 REMARK 620 5 HOH B 918 O 78.6 64.3 94.0 107.8 REMARK 620 6 HOH B1124 O 83.8 80.5 98.8 102.4 142.1 REMARK 620 N 1 2 3 4 5 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 NA B 18 NA REMARK 620 N RES CSSEQI ATOM REMARK 620 1 HOH B 294 O REMARK 620 2 HOH B 622 O 88.1 REMARK 620 3 HOH B 697 O 113.1 85.6 REMARK 620 4 HOH B2231 O 82.3 154.5 76.7 REMARK 620 N 1 2 3 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 NA B 19 NA REMARK 620 N RES CSSEQI ATOM REMARK 620 1 HOH B 715 O REMARK 620 2 HOH B 897 O 81.3 REMARK 620 3 HOH B 904 O 108.2 100.1 REMARK 620 4 HOH B1093 O 78.8 96.1 163.1 REMARK 620 5 HOH B1381 O 156.0 76.8 85.4 93.7 REMARK 620 6 HOH B1692 O 107.0 170.9 81.0 82.2 94.3 REMARK 620 N 1 2 3 4 5 REMARK 800 REMARK 800 SITE REMARK 800 SITE_IDENTIFIER: AC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NGM A 13 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA B 15 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 16 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA B 17 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC5 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA B 18 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC6 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA B 19 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC7 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA B 20 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC8 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 21 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC9 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA B 22 REMARK 800 REMARK 800 SITE_IDENTIFIER: BC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA B 23 DBREF 1QCH A 1 6 PDB 1QCH 1QCH 1 6 DBREF 1QCH B 7 12 PDB 1QCH 1QCH 7 12 SEQRES 1 A 6 DA DT DG DC DA DT SEQRES 1 B 6 DA DT DG DC DA DT HET NGM A 13 106 HET NA A 16 1 HET NA A 21 1 HET NA B 15 1 HET NA B 17 1 HET NA B 18 1 HET NA B 19 1 HET NA B 20 1 HET NA B 22 1 HET NA B 23 1 HETNAM NGM NOGALAMYCIN HETNAM NA SODIUM ION FORMUL 3 NGM C39 H49 N O16 FORMUL 4 NA 9(NA 1+) FORMUL 13 HOH *2227(H2 O) LINK O2 DT A 6 NA NA A 21 1555 1555 2.40 LINK NA NA A 16 O HOH A1143 1555 1555 2.38 LINK NA NA A 16 O HOH A1696 1555 1555 2.33 LINK NA NA A 16 O HOH A2229 1555 1555 2.35 LINK NA NA A 16 O HOH B1305 1555 1555 2.32 LINK NA NA A 21 O HOH A 366 1555 1555 2.53 LINK NA NA A 21 O2 DT B 8 1555 1555 2.36 LINK NA NA A 21 O HOH B 200 1555 1555 2.37 LINK NA NA A 21 O HOH B1045 1555 1555 2.48 LINK NA NA A 21 O HOH B1153 1555 1555 2.42 LINK O HOH A 24 NA NA B 20 1555 1555 2.38 LINK O HOH A 30 NA NA B 15 1555 1555 2.49 LINK O HOH A 85 NA NA B 17 1555 1555 2.38 LINK O HOH A 263 NA NA B 15 1555 1555 2.44 LINK O HOH A 572 NA NA B 20 1555 1555 2.45 LINK O HOH A 574 NA NA B 23 1555 1555 2.36 LINK O HOH A 643 NA NA B 23 1555 1555 2.36 LINK O HOH A 764 NA NA B 23 1555 1555 2.49 LINK O HOH A 778 NA NA B 17 1555 1555 2.39 LINK O HOH A 779 NA NA B 23 1555 1555 2.43 LINK O HOH A 794 NA NA B 23 1555 1555 2.46 LINK O HOH A 814 NA NA B 22 1555 1555 2.38 LINK O HOH A1096 NA NA B 20 1555 1555 2.59 LINK O HOH A1242 NA NA B 17 1555 1555 2.36 LINK O HOH A1473 NA NA B 23 1555 1555 2.62 LINK O HOH A1554 NA NA B 17 1555 1555 2.55 LINK O HOH A1658 NA NA B 17 1555 1555 2.45 LINK O HOH A1977 NA NA B 20 1555 1555 2.49 LINK O HOH A2035 NA NA B 20 1555 1555 2.46 LINK NA NA B 15 O HOH B 563 1555 1555 2.42 LINK NA NA B 15 O HOH B1186 1555 1555 2.36 LINK NA NA B 15 O HOH B1259 1555 1555 2.34 LINK NA NA B 15 O HOH B1498 1555 1555 2.43 LINK NA NA B 17 O HOH B1542 1555 1555 2.39 LINK NA NA B 18 O HOH B 294 1555 1555 2.43 LINK NA NA B 18 O HOH B 622 1555 1555 2.40 LINK NA NA B 18 O HOH B 697 1555 1555 2.44 LINK NA NA B 18 O HOH B2231 1555 1555 2.37 LINK NA NA B 19 O HOH B 715 1555 1555 2.39 LINK NA NA B 19 O HOH B 897 1555 1555 2.44 LINK NA NA B 19 O HOH B 904 1555 1555 2.38 LINK NA NA B 19 O HOH B1093 1555 1555 2.39 LINK NA NA B 19 O HOH B1381 1555 1555 2.39 LINK NA NA B 19 O HOH B1692 1555 1555 2.46 LINK NA NA B 20 O HOH B 548 1555 1555 2.37 LINK NA NA B 22 O HOH B 319 1555 1555 2.57 LINK NA NA B 22 O HOH B 413 1555 1555 2.38 LINK NA NA B 22 O HOH B 482 1555 1555 2.34 LINK NA NA B 22 O HOH B 918 1555 1555 2.48 LINK NA NA B 22 O HOH B1124 1555 1555 2.45 SITE 1 AC1 23 DT A 2 DG A 3 DC A 4 DA A 5 SITE 2 AC1 23 HOH A 165 HOH A 190 HOH A 221 HOH A 354 SITE 3 AC1 23 HOH A 653 HOH A 724 HOH A1519 HOH A1575 SITE 4 AC1 23 HOH A1627 HOH A1642 HOH A1650 HOH A1901 SITE 5 AC1 23 HOH A2034 HOH A2072 DG B 9 DC B 10 SITE 6 AC1 23 DA B 11 HOH B 603 HOH B1309 SITE 1 AC2 6 HOH A 30 HOH A 263 HOH B 563 HOH B1186 SITE 2 AC2 6 HOH B1259 HOH B1498 SITE 1 AC3 4 HOH A1143 HOH A1696 HOH A2229 HOH B1305 SITE 1 AC4 6 HOH A 85 HOH A 778 HOH A1242 HOH A1554 SITE 2 AC4 6 HOH A1658 HOH B1542 SITE 1 AC5 4 HOH B 294 HOH B 622 HOH B 697 HOH B2231 SITE 1 AC6 6 HOH B 715 HOH B 897 HOH B 904 HOH B1093 SITE 2 AC6 6 HOH B1381 HOH B1692 SITE 1 AC7 6 HOH A 24 HOH A 572 HOH A1096 HOH A1977 SITE 2 AC7 6 HOH A2035 HOH B 548 SITE 1 AC8 6 DT A 6 HOH A 366 DT B 8 HOH B 200 SITE 2 AC8 6 HOH B1045 HOH B1153 SITE 1 AC9 6 HOH A 814 HOH B 319 HOH B 413 HOH B 482 SITE 2 AC9 6 HOH B 918 HOH B1124 SITE 1 BC1 6 HOH A 574 HOH A 643 HOH A 764 HOH A 779 SITE 2 BC1 6 HOH A 794 HOH A1473 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
Complete list - 2 20 Bytes