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[Jmol-commits] CVS: Jmol/samples/pdb 1HJE.pdb,NONE,1.1
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From: Miguel <mig...@us...> - 2005-06-05 15:23:33
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Update of /cvsroot/jmol/Jmol/samples/pdb In directory sc8-pr-cvs1.sourceforge.net:/tmp/cvs-serv31408/samples/pdb Added Files: 1HJE.pdb Log Message: Good example of alternate locations --- NEW FILE: 1HJE.pdb --- HEADER CONOTOXIN 15-JAN-01 1HJE TITLE CRYSTAL STRUCTURE OF ALPHA-CONOTOXIN SI COMPND MOL_ID: 1; COMPND 2 MOLECULE: ALPHA-CONOTOXIN SI; COMPND 3 CHAIN: A; COMPND 4 SYNONYM: SI (2-7,3-13); COMPND 5 FRAGMENT: RESIDUES 50-62; COMPND 6 OTHER_DETAILS: AMIDATED C-TERMINUS SOURCE MOL_ID: 1; SOURCE 2 SYNTHETIC: YES; SOURCE 3 ORGANISM_SCIENTIFIC: CONUS STRIATUS; SOURCE 4 ORGANISM_COMMON: STRIATED CONE; SOURCE 5 ORGAN: VENOM DUCT; SOURCE 6 SECRETION: VENOM COMPONENT; SOURCE 7 OTHER_DETAILS: SYNTHESISED BY SOLID PHASE PEPTIDE SOURCE 8 CHEMISTRY KEYWDS CONOTOXIN, NICOTINIC ACETYLCHOLINE RECEPTOR, TOXIN, VENOM EXPDTA X-RAY DIFFRACTION AUTHOR R.W.JANES,B.HARGITTAI,G.BARANY,E.J.MACLEAN,S.J.TEAT REVDAT 1 26-JUN-03 1HJE 0 JRNL AUTH R.W.JANES,B.HARGITTAI,G.BARANY,E.J.MACLEAN, JRNL AUTH 2 S.J.TEAT JRNL TITL THE HIGH RESOLUTION CRYSTAL STRUCTURE OF JRNL TITL 2 ALPHA-CONOTOXIN SI TO 0.75 ANGSTROMS JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. 0.75 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : SHELXL-97 REMARK 3 AUTHORS : G.M.SHELDRICK REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 0.75 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 10.91 REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.5 REMARK 3 COMPLETENESS FOR RANGE (%) : 97.9 REMARK 3 CROSS-VALIDATION METHOD : NONE REMARK 3 FREE R VALUE TEST SET SELECTION : NULL REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT (NO CUTOFF). REMARK 3 R VALUE (WORKING + TEST SET, NO CUTOFF) : NULL REMARK 3 R VALUE (WORKING SET, NO CUTOFF) : 0.1270 REMARK 3 FREE R VALUE (NO CUTOFF) : NONE REMARK 3 FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : NONE REMARK 3 FREE R VALUE TEST SET COUNT (NO CUTOFF) : NONE REMARK 3 TOTAL NUMBER OF REFLECTIONS (NO CUTOFF) : 133616 REMARK 3 REMARK 3 FIT/AGREEMENT OF MODEL FOR DATA WITH F>4SIG(F). REMARK 3 R VALUE (WORKING + TEST SET, F>4SIG(F)) : NULL REMARK 3 R VALUE (WORKING SET, F>4SIG(F)) : 0.1145 REMARK 3 FREE R VALUE (F>4SIG(F)) : NULL REMARK 3 FREE R VALUE TEST SET SIZE (%, F>4SIG(F)) : NULL REMARK 3 FREE R VALUE TEST SET COUNT (F>4SIG(F)) : NULL REMARK 3 TOTAL NUMBER OF REFLECTIONS (F>4SIG(F)) : 15363 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 111 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 6 REMARK 3 SOLVENT ATOMS : 27 REMARK 3 REMARK 3 MODEL REFINEMENT. REMARK 3 OCCUPANCY SUM OF NON-HYDROGEN ATOMS : 102.71 REMARK 3 OCCUPANCY SUM OF HYDROGEN ATOMS : 78.00 REMARK 3 NUMBER OF DISCRETELY DISORDERED RESIDUES : 5 REMARK 3 NUMBER OF LEAST-SQUARES PARAMETERS : 1171 REMARK 3 NUMBER OF RESTRAINTS : 50 REMARK 3 REMARK 3 RMS DEVIATIONS FROM RESTRAINT TARGET VALUES. REMARK 3 BOND LENGTHS (A) : NONE REMARK 3 ANGLE DISTANCES (A) : NONE REMARK 3 SIMILAR DISTANCES (NO TARGET VALUES) (A) : NULL REMARK 3 DISTANCES FROM RESTRAINT PLANES (A) : NULL REMARK 3 ZERO CHIRAL VOLUMES (A**3) : NULL REMARK 3 NON-ZERO CHIRAL VOLUMES (A**3) : NULL REMARK 3 ANTI-BUMPING DISTANCE RESTRAINTS (A) : NULL REMARK 3 RIGID-BOND ADP COMPONENTS (A**2) : NULL REMARK 3 SIMILAR ADP COMPONENTS (A**2) : NULL REMARK 3 APPROXIMATELY ISOTROPIC ADPS (A**2) : NULL REMARK 3 REMARK 3 BULK SOLVENT MODELING. REMARK 3 METHOD USED: NONE REMARK 3 REMARK 3 STEREOCHEMISTRY TARGET VALUES : NONE REMARK 3 SPECIAL CASE: NULL REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: XTALVIEW REMARK 4 REMARK 4 1HJE COMPLIES WITH FORMAT V. 2.3, 09-JULY-1998 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY EBI ON 16-JAN-2001. REMARK 100 THE EBI ID CODE IS EBI-5678. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 15-JUL-2000 REMARK 200 TEMPERATURE (KELVIN) : 150 REMARK 200 PH : NULL REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : SRS BEAMLINE PX9.8 REMARK 200 BEAMLINE : PX9.8 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.6887 REMARK 200 MONOCHROMATOR : SILICON 111 REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : SMART 1K CCD REMARK 200 DETECTOR MANUFACTURER : BRUKER AXS REMARK 200 INTENSITY-INTEGRATION SOFTWARE : SAINT REMARK 200 DATA SCALING SOFTWARE : SADABS REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 21312 REMARK 200 RESOLUTION RANGE HIGH (A) : 0.75 REMARK 200 RESOLUTION RANGE LOW (A) : 10.91 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.0 REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 97.9 REMARK 200 DATA REDUNDANCY : 5.99 REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : 0.0612 REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 19.65 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 0.75 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 0.87 REMARK 200 COMPLETENESS FOR SHELL (%) : 96.3 REMARK 200 DATA REDUNDANCY IN SHELL : 3.30 REMARK 200 R MERGE FOR SHELL (I) : NULL REMARK 200 R SYM FOR SHELL (I) : 0.2635 REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.07 REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: DIRECT METHODS REMARK 200 SOFTWARE USED: SHELX REMARK 200 STARTING MODEL: NULL REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 23.64 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.61 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 0.4M K,NA TARTRATE REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 65 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -Y,X-Y,Z+2/3 REMARK 290 3555 Y-X,-X,Z+1/3 REMARK 290 4555 -X,-Y,Z+1/2 REMARK 290 5555 Y,Y-X,Z+1/6 REMARK 290 6555 X-Y,X,Z+5/6 REMARK 290 REMARK 290 WHERE NNN -> OPERATOR NUMBER REMARK 290 MMM -> TRANSLATION VECTOR REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY REMARK 290 RELATED MOLECULES. REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 2 -0.500000 -0.866025 0.000000 0.00000 REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 9.77933 REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000 REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000 REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 4.88967 REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 7.33450 REMARK 290 SMTRY1 5 0.500000 0.866025 0.000000 0.00000 REMARK 290 SMTRY2 5 -0.866025 0.500000 0.000000 0.00000 REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 2.44483 REMARK 290 SMTRY1 6 0.500000 -0.866025 0.000000 0.00000 REMARK 290 SMTRY2 6 0.866025 0.500000 0.000000 0.00000 REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 12.22417 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1 REMARK 300 THIS ENTRY CONTAINS THE CRYSTALLOGRAPHIC ASYMMETRIC UNIT REMARK 300 WHICH CONSISTS OF 1 CHAIN(S). SEE REMARK 350 FOR REMARK 300 INFORMATION ON GENERATING THE BIOLOGICAL MOLECULE(S). REMARK 350 REMARK 350 GENERATING THE BIOMOLECULE 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 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 400 REMARK 400 COMPOUND REMARK 400 ALPHA-CONOTOXINS BIND TO THE NICOTINIC ACETYLCHOLINE RECEPTORS REMARK 400 (NACHR) AND INHIBIT THEM. REMARK 525 REMARK 525 SOLVENT REMARK 525 REMARK 525 THE SOLVENT MOLECULES ARE GIVEN CHAIN IDENTIFIERS TO REMARK 525 INDICATE THE PROTEIN CHAIN TO WHICH THEY ARE MOST CLOSELY REMARK 525 ASSOCIATED WITH: REMARK 525 PROTEIN CHAIN SOLVENT CHAIN REMARK 525 A Z REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 1QMW RELATED DB: PDB REMARK 900 SOLUTION STRUCTURE OF ALPHA-CONOTOXIN SI DBREF 1HJE A 1 13 SWS P15471 CXA1_CONST 50 62 DBREF 1HJE A 14 14 PDB 1HJE 1HJE 14 14 SEQRES 1 A 14 ILE CYS CYS ASN PRO ALA CYS GLY PRO LYS TYR SER CYS SEQRES 2 A 14 NH2 HET NH2 A 14 2 HETNAM NH2 AMINO GROUP FORMUL 2 NH2 H2 N1 FORMUL 3 HOH *27(H2 O1) HELIX 1 1 ASN A 4 GLY A 8 5 5 HELIX 2 2 CYS A 7 TYR A 11 5 5 SSBOND 1 CYS A 2 CYS A 7 1555 1555 SSBOND 2 CYS A 3 CYS A 13 1555 1555 LINK C ACYS A 13 N ANH2 A 14 1555 1555 LINK C BCYS A 13 N ANH2 A 14 1555 1555 LINK C ACYS A 13 N BNH2 A 14 1555 1555 LINK C BCYS A 13 N BNH2 A 14 1555 1555 CRYST1 32.092 32.092 14.669 90.00 90.00 120.00 P 65 6 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 0.031161 0.017991 0.000000 0.00000 SCALE2 0.000000 0.035981 0.000000 0.00000 SCALE3 0.000000 0.000000 0.068171 0.00000 ATOM 1 N AILE A 1 4.680 -3.824 -0.511 0.53 15.99 N ANISOU 1 N AILE A 1 661 2592 2822 308 186 -1374 N ATOM 2 CA AILE A 1 6.185 -4.007 -0.275 0.47 8.68 C ANISOU 2 CA AILE A 1 834 1075 1387 183 137 -121 C ATOM 3 C AILE A 1 6.838 -4.518 -1.492 0.47 6.66 C ANISOU 3 C AILE A 1 572 669 1291 79 1 -109 C ATOM 4 O AILE A 1 6.165 -4.996 -2.395 0.47 8.20 O ANISOU 4 O AILE A 1 492 1114 1510 69 -63 -98 O ATOM 5 CB AILE A 1 6.516 -4.682 1.002 0.53 29.26 C ANISOU 5 CB AILE A 1 1458 5249 4411 -535 1309 -3563 C ATOM 6 CG1AILE A 1 6.489 -6.193 1.059 0.53 12.00 C ANISOU 6 CG1AILE A 1 1732 1418 1409 -878 27 -219 C ATOM 7 CG2AILE A 1 5.758 -4.058 2.220 0.53 75.10 C ANISOU 7 CG2AILE A 1 17052 2701 8781 802 11587 -327 C ATOM 8 CD1AILE A 1 7.226 -6.793 2.256 0.53 27.65 C ATOM 9 H1 AILE A 1 4.167 -3.523 0.137 0.53 19.19 H ATOM 10 H2 AILE A 1 4.331 -4.020 -1.295 0.53 19.19 H ATOM 11 HA AILE A 1 6.540 -3.078 -0.170 0.53 10.41 H ATOM 12 HB AILE A 1 7.474 -4.447 1.163 0.53 35.11 H ATOM 13 1HG1AILE A 1 5.546 -6.493 1.085 0.53 14.40 H ATOM 14 2HG1AILE A 1 6.894 -6.549 0.228 0.53 14.40 H ATOM 15 1HG2AILE A 1 5.612 -3.102 2.059 0.53 90.12 H ATOM 16 2HG2AILE A 1 4.894 -4.506 2.331 0.53 90.12 H ATOM 17 3HG2AILE A 1 6.294 -4.174 3.032 0.53 90.12 H ATOM 18 1HD1AILE A 1 7.826 -6.120 2.641 0.53 33.18 H ATOM 19 2HD1AILE A 1 6.576 -7.075 2.933 0.53 33.18 H ATOM 20 3HD1AILE A 1 7.750 -7.568 1.963 0.53 33.18 H ATOM 21 N BILE A 1 5.330 -2.842 -0.592 0.47 9.70 N ANISOU 21 N BILE A 1 784 1213 1690 360 345 169 N ATOM 22 CA BILE A 1 6.185 -4.007 -0.275 0.47 8.68 C ANISOU 22 CA BILE A 1 834 1075 1387 183 137 -121 C ATOM 23 C BILE A 1 6.838 -4.518 -1.492 0.47 6.66 C ANISOU 23 C BILE A 1 572 669 1291 79 1 -109 C ATOM 24 O BILE A 1 6.165 -4.996 -2.395 0.47 8.20 O ANISOU 24 O BILE A 1 492 1114 1510 69 -63 -98 O ATOM 25 CB BILE A 1 5.643 -5.167 0.513 0.47 6.79 C ANISOU 25 CB BILE A 1 448 1219 911 -133 204 -66 C ATOM 26 CG1BILE A 1 4.950 -4.759 1.816 0.47 10.97 C ANISOU 26 CG1BILE A 1 988 1354 1827 -46 676 77 C ATOM 27 CG2BILE A 1 6.720 -6.250 0.772 0.47 8.77 C ANISOU 27 CG2BILE A 1 1270 962 1102 -92 358 324 C ATOM 28 CD1BILE A 1 5.894 -4.131 2.826 0.47 11.72 C ANISOU 28 CD1BILE A 1 1132 2132 1191 -279 519 -671 C ATOM 29 H1 BILE A 1 4.881 -2.439 0.048 0.47 11.64 H ATOM 30 H2 BILE A 1 5.271 -2.553 -1.421 0.47 11.64 H ATOM 31 HA BILE A 1 6.929 -3.639 0.283 0.47 10.41 H ATOM 32 HB BILE A 1 4.943 -5.595 -0.058 0.47 8.14 H ATOM 33 1HG1BILE A 1 4.228 -4.115 1.608 0.47 13.17 H ATOM 34 2HG1BILE A 1 4.532 -5.560 2.222 0.47 13.17 H ATOM 35 1HG2BILE A 1 7.273 -6.358 -0.030 0.47 10.53 H ATOM 36 2HG2BILE A 1 7.285 -5.976 1.524 0.47 10.53 H ATOM 37 3HG2BILE A 1 6.283 -7.101 0.984 0.47 10.53 H ATOM 38 1HD1BILE A 1 6.755 -4.599 2.803 0.47 14.07 H ATOM 39 2HD1BILE A 1 6.029 -3.186 2.604 0.47 14.07 H ATOM 40 3HD1BILE A 1 5.507 -4.203 3.724 0.47 14.07 H ATOM 41 N CYS A 2 8.168 -4.430 -1.534 1.00 5.91 N ANISOU 41 N CYS A 2 551 639 1054 17 -32 -10 N ATOM 42 CA CYS A 2 8.906 -4.959 -2.668 1.00 5.22 C ANISOU 42 CA CYS A 2 481 466 1037 -37 -69 -26 C ATOM 43 C CYS A 2 10.316 -5.182 -2.126 1.00 4.56 C ANISOU 43 C CYS A 2 499 451 782 -52 -17 3 C ATOM 44 O CYS A 2 11.166 -4.306 -2.159 1.00 5.16 O ANISOU 44 O CYS A 2 579 436 944 -105 -86 71 O ATOM 45 CB CYS A 2 8.869 -3.992 -3.845 1.00 5.94 C ANISOU 45 CB CYS A 2 568 578 1112 17 -154 86 C ATOM 46 SG CYS A 2 9.238 -4.717 -5.466 1.00 6.50 S ANISOU 46 SG CYS A 2 659 786 1024 -157 -163 49 S ATOM 47 H CYS A 2 8.602 -4.049 -0.869 1.00 7.09 H ATOM 48 HA CYS A 2 8.511 -5.835 -2.943 1.00 6.27 H ATOM 49 1HB CYS A 2 7.969 -3.582 -3.884 1.00 7.13 H ATOM 50 2HB CYS A 2 9.519 -3.266 -3.672 1.00 7.13 H ATOM 51 N CYS A 3 10.513 -6.371 -1.530 1.00 4.42 N ANISOU 51 N CYS A 3 446 423 811 -74 5 28 N ATOM 52 CA CYS A 3 11.672 -6.587 -0.676 1.00 4.12 C ANISOU 52 CA CYS A 3 434 433 698 -27 67 12 C ATOM 53 C CYS A 3 12.767 -7.323 -1.458 1.00 3.92 C ANISOU 53 C CYS A 3 422 406 660 -61 -2 2 C ATOM 54 O CYS A 3 13.145 -8.454 -1.177 1.00 4.72 O ANISOU 54 O CYS A 3 529 450 814 8 33 70 O ATOM 55 CB CYS A 3 11.268 -7.325 0.580 1.00 4.89 C ANISOU 55 CB CYS A 3 565 523 769 -38 94 51 C ATOM 56 SG CYS A 3 12.607 -7.439 1.816 1.00 5.79 S ANISOU 56 SG CYS A 3 754 710 734 49 50 112 S ATOM 57 H CYS A 3 9.937 -7.024 -1.657 1.00 5.31 H ATOM 58 HA CYS A 3 12.030 -5.693 -0.409 1.00 4.94 H ATOM 59 1HB CYS A 3 10.494 -6.863 0.988 1.00 5.87 H ATOM 60 2HB CYS A 3 10.979 -8.239 0.335 1.00 5.87 H ATOM 61 N ASN A 4 13.293 -6.621 -2.461 1.00 4.55 N ANISOU 61 N ASN A 4 552 426 752 58 130 70 N ATOM 62 CA ASN A 4 14.332 -7.175 -3.319 1.00 4.47 C ANISOU 62 CA ASN A 4 531 494 672 57 72 70 C ATOM 63 C ASN A 4 15.046 -5.975 -3.950 1.00 4.38 C ANISOU 63 C ASN A 4 568 478 619 6 62 34 C ATOM 64 O ASN A 4 14.364 -5.053 -4.377 1.00 4.54 O ANISOU 64 O ASN A 4 536 467 722 14 85 16 O ATOM 65 CB ASN A 4 13.733 -8.064 -4.421 1.00 4.84 C ANISOU 65 CB ASN A 4 584 451 803 32 22 27 C ATOM 66 CG ASN A 4 14.819 -8.796 -5.176 1.00 4.67 C ANISOU 66 CG ASN A 4 629 476 671 -21 -29 -29 C ATOM 67 OD1 ASN A 4 15.576 -8.210 -5.947 1.00 6.24 O ANISOU 67 OD1 ASN A 4 900 562 910 -15 241 -33 O ATOM 68 ND2 ASN A 4 14.956 -10.089 -4.899 1.00 5.15 N ANISOU 68 ND2 ASN A 4 696 481 779 62 33 -41 N ATOM 69 H ASN A 4 13.005 -5.803 -2.609 1.00 5.46 H ATOM 70 HA ASN A 4 14.979 -7.704 -2.770 1.00 5.36 H ATOM 71 1HB ASN A 4 13.114 -8.721 -4.014 1.00 5.81 H ATOM 72 2HB ASN A 4 13.214 -7.503 -5.050 1.00 5.81 H ATOM 73 1HD2 ASN A 4 15.604 -10.552 -5.272 1.00 6.18 H ATOM 74 2HD2 ASN A 4 14.399 -10.481 -4.343 1.00 6.18 H ATOM 75 N PRO A 5 16.371 -5.951 -4.019 1.00 4.98 N ANISOU 75 N PRO A 5 542 605 744 29 62 50 N ATOM 76 CA PRO A 5 17.037 -4.769 -4.582 1.00 5.18 C ANISOU 76 CA PRO A 5 568 644 757 -74 67 -14 C ATOM 77 C PRO A 5 16.635 -4.444 -5.979 1.00 4.92 C ANISOU 77 C PRO A 5 545 580 746 -50 126 -30 C ATOM 78 O PRO A 5 16.694 -3.276 -6.378 1.00 5.94 O ANISOU 78 O PRO A 5 744 558 955 -186 -21 134 O ATOM 79 HA PRO A 5 16.829 -3.981 -4.001 1.00 6.22 H ATOM 80 CB APRO A 5 18.553 -5.124 -4.411 0.76 7.76 C ANISOU 80 CB APRO A 5 595 1459 895 -21 -46 -69 C ATOM 81 CG APRO A 5 18.598 -6.179 -3.402 0.76 6.21 C ANISOU 81 CG APRO A 5 478 883 999 44 -7 -10 C ATOM 82 CD APRO A 5 17.360 -7.013 -3.563 0.76 7.47 C ANISOU 82 CD APRO A 5 828 1004 1004 206 -92 -42 C ATOM 83 1HB APRO A 5 18.935 -5.443 -5.267 0.76 9.31 H ATOM 84 2HB APRO A 5 19.065 -4.331 -4.110 0.76 9.31 H ATOM 85 1HG APRO A 5 19.405 -6.738 -3.528 0.76 7.46 H ATOM 86 2HG APRO A 5 18.628 -5.784 -2.495 0.76 7.46 H ATOM 87 1HD APRO A 5 17.480 -7.719 -4.248 0.76 8.96 H ATOM 88 2HD APRO A 5 17.084 -7.428 -2.708 0.76 8.96 H ATOM 89 CB BPRO A 5 18.518 -5.147 -4.582 0.23 3.56 C ANISOU 89 CB BPRO A 5 373 379 601 -112 89 96 C ATOM 90 CG BPRO A 5 18.652 -6.523 -4.116 0.23 10.72 C ANISOU 90 CG BPRO A 5 1113 1238 1721 148 77 -267 C ATOM 91 CD BPRO A 5 17.313 -6.945 -3.595 0.23 4.28 C ANISOU 91 CD BPRO A 5 144 532 949 46 81 546 C ATOM 92 1HB BPRO A 5 18.887 -5.063 -5.497 0.23 4.27 H ATOM 93 2HB BPRO A 5 19.022 -4.538 -3.987 0.23 4.27 H ATOM 94 1HG BPRO A 5 18.932 -7.113 -4.861 0.23 12.86 H ATOM 95 2HG BPRO A 5 19.332 -6.578 -3.398 0.23 12.86 H ATOM 96 1HD BPRO A 5 17.065 -7.832 -3.960 0.23 5.13 H ATOM 97 2HD BPRO A 5 17.330 -7.003 -2.607 0.23 5.13 H ATOM 98 N ALA A 6 16.195 -5.429 -6.762 1.00 4.86 N ANISOU 98 N ALA A 6 619 481 746 -42 161 9 N ATOM 99 CA ALA A 6 15.743 -5.172 -8.115 1.00 5.45 C ANISOU 99 CA ALA A 6 714 652 703 -88 171 -43 C ATOM 100 C ALA A 6 14.498 -4.299 -8.165 1.00 5.46 C ANISOU 100 C ALA A 6 820 542 711 -115 -38 10 C ATOM 101 O ALA A 6 14.179 -3.744 -9.212 1.00 7.57 O ANISOU 101 O ALA A 6 1153 930 794 5 -42 98 O ATOM 102 CB ALA A 6 15.473 -6.474 -8.849 1.00 6.78 C ANISOU 102 CB ALA A 6 968 784 826 -3 138 -194 C ATOM 103 H ALA A 6 16.178 -6.252 -6.450 1.00 5.83 H ATOM 104 HA ALA A 6 16.476 -4.692 -8.598 1.00 6.54 H ATOM 105 1HB ALA A 6 14.733 -6.946 -8.415 1.00 8.14 H ATOM 106 2HB ALA A 6 15.236 -6.280 -9.780 1.00 8.14 H ATOM 107 3HB ALA A 6 16.277 -7.034 -8.826 1.00 8.14 H ATOM 108 N CYS A 7 13.792 -4.189 -7.038 1.00 4.85 N ANISOU 108 N CYS A 7 648 444 751 -54 9 -28 N ATOM 109 CA CYS A 7 12.654 -3.287 -6.932 1.00 5.27 C ANISOU 109 CA CYS A 7 665 435 903 -93 -81 19 C ATOM 110 C CYS A 7 13.059 -1.812 -7.074 1.00 5.11 C ANISOU 110 C CYS A 7 723 465 753 -67 -27 16 C ATOM 111 O CYS A 7 12.205 -0.980 -7.307 1.00 5.67 O ANISOU 111 O CYS A 7 726 471 957 -11 -78 71 O ATOM 112 CB CYS A 7 11.972 -3.474 -5.578 1.00 5.13 C ANISOU 112 CB CYS A 7 566 444 938 -63 11 3 C ATOM 113 SG CYS A 7 11.228 -5.129 -5.382 1.00 6.00 S ANISOU 113 SG CYS A 7 673 486 1119 -82 14 62 S ATOM 114 H CYS A 7 14.020 -4.674 -6.341 1.00 5.82 H ATOM 115 HA CYS A 7 12.000 -3.510 -7.655 1.00 6.32 H ATOM 116 1HB CYS A 7 12.637 -3.332 -4.859 1.00 6.15 H ATOM 117 2HB CYS A 7 11.265 -2.788 -5.476 1.00 6.15 H ATOM 118 N GLY A 8 14.342 -1.509 -6.882 1.00 5.94 N ANISOU 118 N GLY A 8 667 449 1141 -82 8 24 N ATOM 119 CA GLY A 8 14.818 -0.160 -7.139 1.00 6.64 C ANISOU 119 CA GLY A 8 788 487 1249 -123 125 9 C ATOM 120 C GLY A 8 14.110 0.845 -6.272 1.00 5.52 C ANISOU 120 C GLY A 8 711 410 975 -127 -77 69 C ATOM 121 O GLY A 8 14.087 0.686 -5.056 1.00 6.18 O ANISOU 121 O GLY A 8 898 513 938 -39 -134 165 O ATOM 122 H GLY A 8 14.901 -2.126 -6.600 1.00 7.13 H ATOM 123 1HA GLY A 8 14.670 0.065 -8.091 1.00 7.97 H ATOM 124 2HA GLY A 8 15.792 -0.117 -6.963 1.00 7.97 H ATOM 125 N PRO A 9 13.488 1.890 -6.857 1.00 5.59 N ANISOU 125 N PRO A 9 808 484 831 -142 -68 137 N ATOM 126 CA PRO A 9 12.842 2.907 -6.035 1.00 5.95 C ANISOU 126 CA PRO A 9 944 375 943 -46 -143 98 C ATOM 127 C PRO A 9 11.660 2.394 -5.231 1.00 5.44 C ANISOU 127 C PRO A 9 827 394 847 95 -113 102 C ATOM 128 O PRO A 9 11.208 3.091 -4.309 1.00 6.34 O ANISOU 128 O PRO A 9 982 389 1039 104 16 35 O ATOM 129 HA PRO A 9 13.515 3.307 -5.414 1.00 7.15 H ATOM 130 CB APRO A 9 12.435 3.963 -7.105 0.51 8.19 C ANISOU 130 CB APRO A 9 1682 381 1049 230 -339 393 C ATOM 131 CG APRO A 9 12.195 3.159 -8.277 0.51 6.50 C ANISOU 131 CG APRO A 9 908 607 956 -331 -298 399 C ATOM 132 CD APRO A 9 13.258 2.121 -8.310 0.51 6.75 C ANISOU 132 CD APRO A 9 1077 628 858 -153 -121 -151 C ATOM 133 1HB APRO A 9 11.618 4.452 -6.833 0.51 9.83 H ATOM 134 2HB APRO A 9 13.165 4.614 -7.261 0.51 9.83 H ATOM 135 1HG APRO A 9 11.302 2.736 -8.228 0.51 7.80 H ATOM 136 2HG APRO A 9 12.235 3.718 -9.093 0.51 7.80 H ATOM 137 1HD APRO A 9 12.947 1.297 -8.764 0.51 8.10 H ATOM 138 2HD APRO A 9 14.075 2.453 -8.759 0.51 8.10 H ATOM 139 CB BPRO A 9 12.504 3.927 -6.993 0.49 9.28 C ANISOU 139 CB BPRO A 9 1158 895 1471 -360 362 42 C ATOM 140 CG BPRO A 9 12.515 3.336 -8.309 0.49 28.62 C ANISOU 140 CG BPRO A 9 4292 4521 2062 3304 1768 2440 C ATOM 141 CD BPRO A 9 13.413 2.146 -8.243 0.49 7.54 C ANISOU 141 CD BPRO A 9 753 1090 1022 -266 10 621 C ATOM 142 1HB BPRO A 9 11.607 4.295 -6.794 0.49 11.13 H ATOM 143 2HB BPRO A 9 13.162 4.665 -6.948 0.49 11.13 H ATOM 144 1HG BPRO A 9 11.600 3.063 -8.571 0.49 34.34 H ATOM 145 2HG BPRO A 9 12.853 3.985 -8.976 0.49 34.34 H ATOM 146 1HD BPRO A 9 13.024 1.376 -8.729 0.49 9.05 H ATOM 147 2HD BPRO A 9 14.306 2.349 -8.618 0.49 9.05 H ATOM 148 N LYS A 10 11.138 1.213 -5.549 1.00 5.38 N ANISOU 148 N LYS A 10 741 422 880 32 -43 88 N ATOM 149 CA LYS A 10 10.031 0.619 -4.833 1.00 5.75 C ANISOU 149 CA LYS A 10 672 529 985 72 -20 104 C ATOM 150 C LYS A 10 10.478 -0.173 -3.603 1.00 5.73 C ANISOU 150 C LYS A 10 800 386 989 -44 -23 55 C ATOM 151 O LYS A 10 9.631 -0.721 -2.898 1.00 6.83 O ANISOU 151 O LYS A 10 760 644 1192 -57 65 233 O ATOM 152 CB LYS A 10 9.251 -0.305 -5.750 1.00 7.11 C ANISOU 152 CB LYS A 10 639 865 1199 -27 -110 26 C ATOM 153 CG LYS A 10 8.686 0.374 -6.976 1.00 11.00 C ANISOU 153 CG LYS A 10 1346 1481 1352 250 -527 -137 C ATOM 154 H LYS A 10 11.482 0.772 -6.228 1.00 6.45 H ATOM 155 HA LYS A 10 9.421 1.352 -4.531 1.00 6.91 H ATOM 156 1HB LYS A 10 9.845 -1.041 -6.041 1.00 8.54 H ATOM 157 2HB LYS A 10 8.505 -0.706 -5.237 1.00 8.54 H ATOM 158 1HG LYS A 10 8.003 1.042 -6.715 1.00 13.20 H ATOM 159 2HG LYS A 10 9.405 0.836 -7.475 1.00 13.20 H ATOM 160 CD ALYS A 10 8.039 -0.747 -7.867 0.40 12.71 C ATOM 161 CE ALYS A 10 7.676 -0.233 -9.229 0.25 14.07 C ATOM 162 NZ ALYS A 10 8.247 -1.112 -10.278 0.25 27.80 N ATOM 163 CD BLYS A 10 8.039 -0.747 -7.867 0.40 12.71 C ATOM 164 CE BLYS A 10 6.807 -0.556 -8.717 0.25 26.94 C ATOM 165 NZ BLYS A 10 6.949 -1.509 -9.852 0.25 14.14 N ATOM 166 N TYR A 11 11.775 -0.262 -3.331 1.00 5.25 N ANISOU 166 N TYR A 11 724 389 881 -40 -20 110 N ATOM 167 CA TYR A 11 12.258 -1.158 -2.280 1.00 5.14 C ANISOU 167 CA TYR A 11 760 381 812 -39 -86 69 C ATOM 168 C TYR A 11 11.595 -0.869 -0.939 1.00 5.37 C ANISOU 168 C TYR A 11 752 424 863 9 -73 33 C ATOM 169 O TYR A 11 11.611 0.274 -0.440 1.00 7.19 O ANISOU 169 O TYR A 11 1304 419 1008 -26 57 -30 O ATOM 170 CB TYR A 11 13.784 -0.982 -2.125 1.00 5.51 C ANISOU 170 CB TYR A 11 743 484 868 -101 -1 125 C ATOM 171 CG TYR A 11 14.393 -2.026 -1.231 1.00 4.87 C ANISOU 171 CG TYR A 11 612 511 727 -165 -53 68 C ATOM 172 CD1 TYR A 11 14.495 -1.917 0.141 1.00 5.52 C ANISOU 172 CD1 TYR A 11 683 502 912 -77 6 -85 C ATOM 173 CD2 TYR A 11 14.876 -3.194 -1.782 1.00 5.60 C ANISOU 173 CD2 TYR A 11 798 607 721 -4 -96 6 C ATOM 174 CE1 TYR A 11 15.073 -2.940 0.927 1.00 5.15 C ANISOU 174 CE1 TYR A 11 663 683 608 -43 -58 -9 C ATOM 175 CE2 TYR A 11 15.448 -4.189 -1.038 1.00 5.68 C ANISOU 175 CE2 TYR A 11 789 606 765 60 -54 -33 C ATOM 176 CZ TYR A 11 15.538 -4.066 0.331 1.00 5.20 C ANISOU 176 CZ TYR A 11 587 574 817 9 2 82 C ATOM 177 OH TYR A 11 16.103 -5.100 1.031 1.00 6.63 O ANISOU 177 OH TYR A 11 873 756 889 190 -79 148 O ATOM 178 H TYR A 11 12.350 0.224 -3.788 1.00 6.30 H ATOM 179 HA TYR A 11 12.064 -2.103 -2.542 1.00 6.17 H ATOM 180 1HB TYR A 11 14.208 -1.031 -3.018 1.00 6.61 H ATOM 181 2HB TYR A 11 13.970 -0.085 -1.750 1.00 6.61 H ATOM 182 HD1 TYR A 11 14.167 -1.134 0.568 1.00 6.62 H ATOM 183 HD2 TYR A 11 14.807 -3.313 -2.722 1.00 6.72 H ATOM 184 HE1 TYR A 11 15.137 -2.839 1.869 1.00 6.17 H ATOM 185 HE2 TYR A 11 15.784 -4.967 -1.466 1.00 6.82 H ATOM 186 HH TYR A 11 16.368 -4.821 1.777 1.00 7.95 H ATOM 187 N SER A 12 11.085 -1.909 -0.325 1.00 5.18 N ANISOU 187 N SER A 12 752 455 760 -54 30 -6 N ATOM 188 CA SER A 12 10.492 -1.825 1.002 1.00 6.08 C ANISOU 188 CA SER A 12 874 587 848 13 68 3 C ATOM 189 C SER A 12 10.301 -3.255 1.508 1.00 5.59 C ANISOU 189 C SER A 12 764 591 767 -66 122 -7 C ATOM 190 O SER A 12 9.883 -4.129 0.763 1.00 6.48 O ANISOU 190 O SER A 12 959 635 869 -116 53 45 O ATOM 191 H SER A 12 11.101 -2.689 -0.731 1.00 6.21 H ATOM 192 HA SER A 12 11.098 -1.321 1.618 1.00 7.29 H ATOM 193 CB ASER A 12 9.111 -1.136 0.933 0.67 9.84 C ANISOU 193 CB ASER A 12 1261 1021 1458 433 412 185 C ATOM 194 OG ASER A 12 8.466 -1.191 2.187 0.67 16.95 O ANISOU 194 OG ASER A 12 1931 2190 2320 1032 1160 344 O ATOM 195 1HB ASER A 12 9.226 -0.191 0.661 0.67 11.81 H ATOM 196 2HB ASER A 12 8.550 -1.585 0.252 0.67 11.81 H ATOM 197 HG ASER A 12 7.714 -0.822 2.131 0.67 20.34 H ATOM 198 CB BSER A 12 9.111 -1.136 0.933 0.33 9.84 C ANISOU 198 CB BSER A 12 1261 1021 1458 433 412 185 C ATOM 199 OG BSER A 12 8.257 -1.663 -0.027 0.33 15.15 O ANISOU 199 OG BSER A 12 1067 1053 3638 -131 -43 -75 O ATOM 200 1HB BSER A 12 8.676 -1.209 1.819 0.33 11.81 H ATOM 201 2HB BSER A 12 9.246 -0.173 0.744 0.33 11.81 H ATOM 202 HG BSER A 12 7.527 -1.248 -0.010 0.33 18.18 H ATOM 203 N CYS A 13 10.582 -3.453 2.786 1.00 6.47 N ANISOU 203 N CYS A 13 1006 670 784 -58 89 1 N ATOM 204 CA CYS A 13 10.428 -4.737 3.423 1.00 7.11 C ANISOU 204 CA CYS A 13 1158 745 796 -111 245 70 C ATOM 205 CB CYS A 13 11.778 -5.324 3.833 1.00 7.60 C ANISOU 205 CB CYS A 13 1397 750 743 -17 49 95 C ATOM 206 SG CYS A 13 12.930 -5.540 2.455 1.00 6.50 S ANISOU 206 SG CYS A 13 876 821 771 -184 -27 64 S ATOM 207 H CYS A 13 10.875 -2.775 3.265 1.00 7.77 H ATOM 208 HA CYS A 13 9.997 -5.362 2.772 1.00 8.53 H ATOM 209 1HB CYS A 13 12.194 -4.728 4.506 1.00 9.13 H ATOM 210 2HB CYS A 13 11.626 -6.202 4.263 1.00 9.13 H ATOM 211 C ACYS A 13 9.556 -4.664 4.668 0.61 10.12 C ANISOU 211 C ACYS A 13 1649 1244 950 -94 388 17 C ATOM 212 O ACYS A 13 9.027 -3.574 5.034 0.61 12.84 O ANISOU 212 O ACYS A 13 2093 1275 1509 341 970 -33 O ATOM 213 C BCYS A 13 9.556 -4.664 4.668 0.39 10.12 C ANISOU 213 C BCYS A 13 1649 1244 950 -94 388 17 C ATOM 214 O BCYS A 13 8.735 -5.586 4.920 0.39 10.15 O ANISOU 214 O BCYS A 13 954 1585 1316 80 398 637 O HETATM 215 N ANH2 A 14 9.544 -5.816 5.372 0.61 11.60 N ANISOU 215 N ANH2 A 14 2164 1049 1195 -24 655 229 N HETATM 216 1HN ANH2 A 14 9.144 -5.849 6.156 0.61 13.92 H HETATM 217 2HN ANH2 A 14 9.936 -6.534 5.048 0.61 13.92 H HETATM 218 N BNH2 A 14 9.974 -3.612 5.409 0.39 9.95 N ANISOU 218 N BNH2 A 14 1267 1406 1106 342 312 119 N HETATM 219 1HN BNH2 A 14 9.657 -3.492 6.221 0.39 11.94 H HETATM 220 2HN BNH2 A 14 10.564 -3.049 5.079 0.39 11.94 H TER 221 NH2 A 14 HETATM 222 O HOH Z 1 5.849 -2.530 -5.025 0.25 23.29 O ANISOU 222 O HOH Z 1 858 5202 2788 -91 -574 1026 O HETATM 223 O HOH Z 2 5.799 -4.121 -5.285 0.31 10.53 O ANISOU 223 O HOH Z 2 1204 1620 1177 -500 -385 489 O HETATM 224 O HOH Z 3 4.295 -1.160 1.235 0.37 23.20 O ANISOU 224 O HOH Z 3 4706 2392 1717 2039 866 -293 O HETATM 225 O HOH Z 4 2.818 -4.169 -1.246 0.70 30.15 O HETATM 226 O HOH Z 5 3.558 0.333 -7.859 0.30 24.84 O HETATM 227 O HOH Z 6 18.550 -2.672 -8.909 0.41 34.57 O ANISOU 227 O HOH Z 6 10755 432 1947 -778 -1704 -12 O HETATM 228 O HOH Z 7 17.773 -1.430 -4.462 0.60 12.08 O ANISOU 228 O HOH Z 7 1158 1215 2216 -211 -43 -614 O HETATM 229 O HOH Z 8 16.598 -0.993 -4.539 0.30 17.94 O HETATM 230 O HOH Z 9 14.579 -0.917 -10.463 0.59 13.70 O ANISOU 230 O HOH Z 9 2028 1172 2005 174 -394 -485 O HETATM 231 O HOH Z 10 14.989 2.329 -2.779 0.59 11.09 O ANISOU 231 O HOH Z 10 1452 772 1989 -337 -506 297 O HETATM 232 O HOH Z 11 16.456 1.018 -3.270 0.41 20.13 O ANISOU 232 O HOH Z 11 2074 4127 1447 -929 -115 1000 O HETATM 233 O HOH Z 12 10.225 1.024 -10.904 1.00 33.89 O ANISOU 233 O HOH Z 12 4666 5883 2326 -3467 -550 480 O HETATM 234 O HOH Z 13 6.867 -1.214 -2.579 1.00 19.86 O ANISOU 234 O HOH Z 13 1294 2773 3477 541 652 289 O HETATM 235 O HOH Z 14 4.427 -3.104 -8.734 0.30 20.27 O HETATM 236 O HOH Z 15 6.851 0.498 -11.513 0.23 22.02 O ANISOU 236 O HOH Z 15 5069 2043 1252 1315 -831 -372 O HETATM 237 O HOH Z 16 13.159 1.355 1.971 0.42 28.89 O ANISOU 237 O HOH Z 16 4935 2739 3302 -2362 460 845 O HETATM 238 O HOH Z 17 17.067 -4.644 3.314 0.49 5.88 O ANISOU 238 O HOH Z 17 1205 502 529 259 -79 15 O HETATM 239 O HOH Z 18 11.738 1.440 2.142 0.58 11.61 O ANISOU 239 O HOH Z 18 1286 1245 1878 -214 -119 568 O HETATM 240 O HOH Z 19 12.172 2.614 -1.697 0.59 8.77 O ANISOU 240 O HOH Z 19 701 1586 1046 -498 -25 191 O HETATM 241 O HOH Z 20 16.500 -3.927 3.661 0.51 25.86 O ANISOU 241 O HOH Z 20 3261 5834 732 767 526 861 O HETATM 242 O HOH Z 21 6.088 -0.031 2.269 0.35 16.25 O ANISOU 242 O HOH Z 21 2672 1706 1795 -53 -158 341 O HETATM 243 O HOH Z 22 5.778 -0.854 1.444 0.22 29.38 O ANISOU 243 O HOH Z 22 2300 1473 7390 1197 3496 1534 O HETATM 244 O HOH Z 23 7.334 -6.725 6.866 0.61 32.67 O ANISOU 244 O HOH Z 23 2336 6293 3783 -2090 -877 3062 O HETATM 245 O HOH Z 24 6.451 -5.275 6.954 0.40 14.25 O ANISOU 245 O HOH Z 24 921 3462 1031 -124 50 -417 O HETATM 246 O HOH Z 25 9.058 -7.863 3.218 0.59 9.74 O ANISOU 246 O HOH Z 25 1169 1306 1226 -442 -273 251 O HETATM 247 O HOH Z 26 12.473 -1.913 4.089 0.15 20.80 O ANISOU 247 O HOH Z 26 5821 492 1591 1080 -1839 -340 O HETATM 248 O HOH Z 27 11.636 -1.257 4.421 0.85 12.42 O ANISOU 248 O HOH Z 27 2713 914 1090 -476 -590 88 O CONECT CONECT CONECT 46 113 CONECT 56 206 CONECT 113 46 CONECT 206 56 CONECT 211 218 215 CONECT 213 215 218 CONECT 215 213 217 216 211 CONECT 216 215 CONECT 217 215 CONECT 218 221 220 213 211 219 CONECT 219 218 CONECT 220 218 CONECT 221 218 MASTER 198 0 1 2 0 0 0 6 247 1 15 2 END |