| HEADER DE NOVO PROTEIN 05-JUL-15 5AWL | |
| TITLE CRYSTAL STRUCTURE OF A MUTANT OF CHIGNOLIN, CLN025 | |
| COMPND MOL_ID: 1; | |
| COMPND 2 MOLECULE: A MUTANT OF CHIGNOLIN, CLN025; | |
| COMPND 3 CHAIN: A; | |
| COMPND 4 ENGINEERED: YES; | |
| COMPND 5 MUTATION: YES | |
| SOURCE MOL_ID: 1; | |
| SOURCE 2 SYNTHETIC: YES; | |
| SOURCE 3 ORGANISM_SCIENTIFIC: SYNTHETIC CONSTRUCT; | |
| SOURCE 4 ORGANISM_TAXID: 32630 | |
| KEYWDS DE NOVO PROTEIN, BETA-HAIRPIN, MINI-PROTEIN, MINIATURE PROTEIN | |
| EXPDTA X-RAY DIFFRACTION | |
| AUTHOR T.AKIBA,M.ISHIMURA,T.ODAHARA,K.HARATA,S.HONDA | |
| REVDAT 3 20-MAR-24 5AWL 1 SOURCE REMARK | |
| REVDAT 2 26-AUG-15 5AWL 1 REMARK | |
| REVDAT 1 12-AUG-15 5AWL 0 | |
| JRNL AUTH S.HONDA,T.AKIBA,Y.S.KATO,Y.SAWADA,M.SEKIJIMA,M.ISHIMURA, | |
| JRNL AUTH 2 A.OOISHI,H.WATANABE,T.ODAHARA,K.HARATA | |
| JRNL TITL CRYSTAL STRUCTURE OF A TEN-AMINO ACID PROTEIN | |
| JRNL REF J.AM.CHEM.SOC. V. 130 15327 2008 | |
| JRNL REFN ESSN 1520-5126 | |
| JRNL PMID 18950166 | |
| JRNL DOI 10.1021/JA8030533 | |
| REMARK 1 | |
| REMARK 1 REFERENCE 1 | |
| REMARK 1 AUTH S.HONDA,K.YAMASAKI,Y.SAWADA,H.MORII | |
| REMARK 1 TITL 10 RESIDUE FOLDED PEPTIDE DESIGNED BY SEGMENT STATISTICS. | |
| REMARK 1 REF STRUCTURE V. 12 1507 2004 | |
| REMARK 1 REFN ISSN 0969-2126 | |
| REMARK 1 PMID 15296744 | |
| REMARK 1 DOI 10.1016/J.STR.2004.05.022 | |
| REMARK 2 | |
| REMARK 2 RESOLUTION. 1.11 ANGSTROMS. | |
| REMARK 3 | |
| REMARK 3 REFINEMENT. | |
| REMARK 3 PROGRAM : CNS | |
| REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE- | |
| REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU, | |
| REMARK 3 : READ,RICE,SIMONSON,WARREN | |
| REMARK 3 | |
| REMARK 3 DATA USED IN REFINEMENT. | |
| REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.11 | |
| REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 16.80 | |
| REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000 | |
| REMARK 3 COMPLETENESS FOR RANGE (%) : 95.7 | |
| REMARK 3 CROSS-VALIDATION METHOD : FREE R-VALUE | |
| REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM | |
| 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) : 0.088 | |
| REMARK 3 FREE R VALUE (NO CUTOFF) : 0.119 | |
| REMARK 3 FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : 10.200 | |
| REMARK 3 FREE R VALUE TEST SET COUNT (NO CUTOFF) : 287 | |
| REMARK 3 TOTAL NUMBER OF REFLECTIONS (NO CUTOFF) : 3087 | |
| REMARK 3 | |
| REMARK 3 FIT/AGREEMENT OF MODEL FOR DATA WITH F>4SIG(F). | |
| REMARK 3 R VALUE (WORKING + TEST SET, F>4SIG(F)) : 0.080 | |
| REMARK 3 R VALUE (WORKING SET, F>4SIG(F)) : 0.081 | |
| REMARK 3 FREE R VALUE (F>4SIG(F)) : 0.113 | |
| REMARK 3 FREE R VALUE TEST SET SIZE (%, F>4SIG(F)) : 10.400 | |
| REMARK 3 FREE R VALUE TEST SET COUNT (F>4SIG(F)) : 253 | |
| REMARK 3 TOTAL NUMBER OF REFLECTIONS (F>4SIG(F)) : 2682 | |
| REMARK 3 | |
| REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. | |
| REMARK 3 PROTEIN ATOMS : 93 | |
| REMARK 3 NUCLEIC ACID ATOMS : 0 | |
| REMARK 3 HETEROGEN ATOMS : 0 | |
| REMARK 3 SOLVENT ATOMS : 12 | |
| REMARK 3 | |
| REMARK 3 MODEL REFINEMENT. | |
| REMARK 3 OCCUPANCY SUM OF NON-HYDROGEN ATOMS : 103.50 | |
| REMARK 3 OCCUPANCY SUM OF HYDROGEN ATOMS : 73.00 | |
| REMARK 3 NUMBER OF DISCRETELY DISORDERED RESIDUES : 0 | |
| REMARK 3 NUMBER OF LEAST-SQUARES PARAMETERS : 940 | |
| REMARK 3 NUMBER OF RESTRAINTS : 1193 | |
| REMARK 3 | |
| REMARK 3 RMS DEVIATIONS FROM RESTRAINT TARGET VALUES. | |
| REMARK 3 BOND LENGTHS (A) : 0.016 | |
| REMARK 3 ANGLE DISTANCES (A) : 0.026 | |
| REMARK 3 SIMILAR DISTANCES (NO TARGET VALUES) (A) : 0.000 | |
| REMARK 3 DISTANCES FROM RESTRAINT PLANES (A) : 0.022 | |
| REMARK 3 ZERO CHIRAL VOLUMES (A**3) : 0.079 | |
| REMARK 3 NON-ZERO CHIRAL VOLUMES (A**3) : 0.100 | |
| REMARK 3 ANTI-BUMPING DISTANCE RESTRAINTS (A) : 0.193 | |
| REMARK 3 RIGID-BOND ADP COMPONENTS (A**2) : 0.006 | |
| REMARK 3 SIMILAR ADP COMPONENTS (A**2) : 0.035 | |
| REMARK 3 APPROXIMATELY ISOTROPIC ADPS (A**2) : 0.110 | |
| REMARK 3 | |
| REMARK 3 BULK SOLVENT MODELING. | |
| REMARK 3 METHOD USED: NULL | |
| REMARK 3 | |
| REMARK 3 STEREOCHEMISTRY TARGET VALUES : ENGH AND HUBER | |
| REMARK 3 SPECIAL CASE: NULL | |
| REMARK 3 | |
| REMARK 3 OTHER REFINEMENT REMARKS: NULL | |
| REMARK 4 | |
| REMARK 4 5AWL COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 | |
| REMARK 100 | |
| REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 10-JUL-15. | |
| REMARK 100 THE DEPOSITION ID IS D_1300000091. | |
| REMARK 200 | |
| REMARK 200 EXPERIMENTAL DETAILS | |
| REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION | |
| REMARK 200 DATE OF DATA COLLECTION : 09-DEC-05 | |
| REMARK 200 TEMPERATURE (KELVIN) : 290 | |
| REMARK 200 PH : 5.0 | |
| REMARK 200 NUMBER OF CRYSTALS USED : 1 | |
| REMARK 200 | |
| REMARK 200 SYNCHROTRON (Y/N) : N | |
| REMARK 200 RADIATION SOURCE : ROTATING ANODE | |
| REMARK 200 BEAMLINE : NULL | |
| REMARK 200 X-RAY GENERATOR MODEL : MACSCIENCE | |
| REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M | |
| REMARK 200 WAVELENGTH OR RANGE (A) : 1.54 | |
| REMARK 200 MONOCHROMATOR : NULL | |
| REMARK 200 OPTICS : OSMIC CONFOCAL MAX-FLUX | |
| REMARK 200 | |
| REMARK 200 DETECTOR TYPE : CCD | |
| REMARK 200 DETECTOR MANUFACTURER : BRUKER SMART 6000 | |
| REMARK 200 INTENSITY-INTEGRATION SOFTWARE : SMART6000 | |
| REMARK 200 DATA SCALING SOFTWARE : SAINTPLUS | |
| REMARK 200 | |
| REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 3094 | |
| REMARK 200 RESOLUTION RANGE HIGH (A) : 1.110 | |
| REMARK 200 RESOLUTION RANGE LOW (A) : 16.800 | |
| REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL | |
| REMARK 200 | |
| REMARK 200 OVERALL. | |
| REMARK 200 COMPLETENESS FOR RANGE (%) : 95.9 | |
| REMARK 200 DATA REDUNDANCY : 6.500 | |
| REMARK 200 R MERGE (I) : 0.05700 | |
| REMARK 200 R SYM (I) : NULL | |
| REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 26.4000 | |
| REMARK 200 | |
| REMARK 200 IN THE HIGHEST RESOLUTION SHELL. | |
| REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.11 | |
| REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.71 | |
| REMARK 200 COMPLETENESS FOR SHELL (%) : 88.9 | |
| REMARK 200 DATA REDUNDANCY IN SHELL : 4.00 | |
| REMARK 200 R MERGE FOR SHELL (I) : 0.20300 | |
| REMARK 200 R SYM FOR SHELL (I) : NULL | |
| REMARK 200 <I/SIGMA(I)> FOR SHELL : 5.000 | |
| REMARK 200 | |
| REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH | |
| REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: AB INITIO PHASING | |
| REMARK 200 SOFTWARE USED: SNB 2.2 | |
| REMARK 200 STARTING MODEL: NULL | |
| REMARK 200 | |
| REMARK 200 REMARK: NULL | |
| REMARK 280 | |
| REMARK 280 CRYSTAL | |
| REMARK 280 SOLVENT CONTENT, VS (%): 14.10 | |
| REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.40 | |
| REMARK 280 | |
| REMARK 280 CRYSTALLIZATION CONDITIONS: USING 2 UL DROP OF PROTEIN AT 5 MG/ML | |
| REMARK 280 IN A SOLUTION OF 35.7 MM SODIUM CITRATE-CITRIC ACID BUFFER (PH | |
| REMARK 280 5.0) CONTAINING 14.5% SATURATED AMMONIUM SULFATE AGAINST A | |
| REMARK 280 CRYSTALLIZATION WELL SOLUTION OF 71.4 MM SODIUM CITRATE-CITRIC | |
| REMARK 280 ACID BUFFER (PH 5.0) CONTAINING 29% SATURATED AMMONIUM SULFATE., | |
| REMARK 280 VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 283K | |
| REMARK 290 | |
| REMARK 290 CRYSTALLOGRAPHIC SYMMETRY | |
| REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2 | |
| REMARK 290 | |
| REMARK 290 SYMOP SYMMETRY | |
| REMARK 290 NNNMMM OPERATOR | |
| REMARK 290 1555 X,Y,Z | |
| REMARK 290 2555 -X,-Y,Z | |
| REMARK 290 3555 -X+1/2,Y+1/2,-Z | |
| REMARK 290 4555 X+1/2,-Y+1/2,-Z | |
| 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 -1.000000 0.000000 0.000000 0.00000 | |
| REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 | |
| REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000 | |
| REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 9.62300 | |
| REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 16.79850 | |
| REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000 | |
| REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 9.62300 | |
| REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 16.79850 | |
| REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000 | |
| REMARK 290 | |
| REMARK 290 REMARK: NULL | |
| 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 375 | |
| REMARK 375 SPECIAL POSITION | |
| REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS | |
| REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL | |
| REMARK 375 POSITIONS. | |
| REMARK 375 | |
| REMARK 375 ATOM RES CSSEQI | |
| REMARK 375 HOH A 105 LIES ON A SPECIAL POSITION. | |
| REMARK 375 HOH A 112 LIES ON A SPECIAL POSITION. | |
| 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 TYR A 1 CB - CG - CD2 ANGL. DEV. = -3.7 DEGREES | |
| REMARK 500 | |
| REMARK 500 REMARK: NULL | |
| REMARK 900 | |
| REMARK 900 RELATED ENTRIES | |
| REMARK 900 RELATED ID: 1UAO RELATED DB: PDB | |
| REMARK 900 NMR STRUCTURE OF DESIGNED PROTEIN, CHIGNOLIN, CONSISTING OF ONLY | |
| REMARK 900 TEN AMINO ACIDS | |
| REMARK 900 RELATED ID: 2RVD RELATED DB: PDB | |
| REMARK 900 NMR STRUCTURE OF A MUTANT OF CHIGNOLIN, CLN025 | |
| REMARK 999 | |
| REMARK 999 SEQUENCE | |
| REMARK 999 THE SEQUENCE OF THIS PROTEIN WAS NOT AVAILABLE AT THE UNIPROT | |
| REMARK 999 KNOWLEDGEBASE DATABASE (UNIPROTKB) AT THE TIME OF DEPOSITION. | |
| DBREF 5AWL A 1 10 PDB 5AWL 5AWL 1 10 | |
| SEQRES 1 A 10 TYR TYR ASP PRO GLU THR GLY THR TRP TYR | |
| FORMUL 2 HOH *12(H2 O) | |
| CRYST1 19.246 33.597 11.551 90.00 90.00 90.00 P 21 21 2 4 | |
| 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 0.051959 0.000000 0.000000 0.00000 | |
| SCALE2 0.000000 0.029765 0.000000 0.00000 | |
| SCALE3 0.000000 0.000000 0.086573 0.00000 | |
| ATOM 1 N TYR A 1 25.824 21.671 10.238 1.00 8.64 N | |
| ANISOU 1 N TYR A 1 1043 1239 1000 -391 -82 -168 N | |
| ATOM 2 CA TYR A 1 24.935 20.652 10.774 1.00 7.05 C | |
| ANISOU 2 CA TYR A 1 874 959 848 -150 -142 73 C | |
| ATOM 3 C TYR A 1 23.729 20.558 9.852 1.00 5.69 C | |
| ANISOU 3 C TYR A 1 651 640 871 69 -92 15 C | |
| ATOM 4 O TYR A 1 23.390 21.602 9.289 1.00 6.82 O | |
| ANISOU 4 O TYR A 1 1096 550 944 -80 -219 69 O | |
| ATOM 5 CB TYR A 1 24.425 21.029 12.167 1.00 10.53 C | |
| ANISOU 5 CB TYR A 1 1050 2114 836 -206 -52 -78 C | |
| ATOM 6 CG TYR A 1 25.525 21.526 13.070 1.00 12.94 C | |
| ANISOU 6 CG TYR A 1 1132 2825 962 -258 -69 -301 C | |
| ATOM 7 CD1 TYR A 1 25.829 22.870 13.275 1.00 15.47 C | |
| ANISOU 7 CD1 TYR A 1 1558 2870 1451 -244 -188 -875 C | |
| ATOM 8 CD2 TYR A 1 26.291 20.564 13.736 1.00 15.46 C | |
| ANISOU 8 CD2 TYR A 1 1280 3172 1420 -249 -474 -90 C | |
| ATOM 9 CE1 TYR A 1 26.870 23.242 14.135 1.00 18.04 C | |
| ANISOU 9 CE1 TYR A 1 1225 3434 2196 -320 -335 -812 C | |
| ATOM 10 CE2 TYR A 1 27.325 20.871 14.577 1.00 17.34 C | |
| ANISOU 10 CE2 TYR A 1 1416 3544 1629 60 -564 -866 C | |
| ATOM 11 CZ TYR A 1 27.577 22.231 14.752 1.00 16.51 C | |
| ANISOU 11 CZ TYR A 1 1332 3627 1315 -31 -172 -1216 C | |
| ATOM 12 OH TYR A 1 28.648 22.620 15.582 1.00 23.32 O | |
| ANISOU 12 OH TYR A 1 2211 3383 3267 -126 -1462 -950 O | |
| ATOM 13 N TYR A 2 23.068 19.430 9.704 1.00 5.68 N | |
| ANISOU 13 N TYR A 2 543 564 1051 30 -34 171 N | |
| ATOM 14 CA TYR A 2 21.801 19.381 9.017 1.00 4.77 C | |
| ANISOU 14 CA TYR A 2 551 418 842 72 51 88 C | |
| ATOM 15 C TYR A 2 20.667 19.519 10.021 1.00 4.55 C | |
| ANISOU 15 C TYR A 2 506 487 737 -17 2 36 C | |
| ATOM 16 O TYR A 2 20.667 18.957 11.087 1.00 6.56 O | |
| ANISOU 16 O TYR A 2 744 926 824 171 80 280 O | |
| ATOM 17 CB TYR A 2 21.648 18.114 8.208 1.00 5.98 C | |
| ANISOU 17 CB TYR A 2 688 538 1048 -45 188 -11 C | |
| ATOM 18 CG TYR A 2 22.553 17.960 7.031 1.00 5.31 C | |
| ANISOU 18 CG TYR A 2 689 498 832 -106 76 -33 C | |
| ATOM 19 CD1 TYR A 2 23.698 17.188 7.095 1.00 6.77 C | |
| ANISOU 19 CD1 TYR A 2 947 627 999 133 199 -12 C | |
| ATOM 20 CD2 TYR A 2 22.271 18.556 5.816 1.00 6.83 C | |
| ANISOU 20 CD2 TYR A 2 1024 687 884 -37 -41 -54 C | |
| ATOM 21 CE1 TYR A 2 24.520 17.039 5.991 1.00 8.06 C | |
| ANISOU 21 CE1 TYR A 2 840 883 1339 98 232 -60 C | |
| ATOM 22 CE2 TYR A 2 23.080 18.377 4.709 1.00 8.18 C | |
| ANISOU 22 CE2 TYR A 2 1563 844 701 -50 42 97 C | |
| ATOM 23 CZ TYR A 2 24.229 17.647 4.778 1.00 8.72 C | |
| ANISOU 23 CZ TYR A 2 1372 881 1061 -191 467 -87 C | |
| ATOM 24 OH TYR A 2 24.977 17.478 3.665 1.00 13.52 O | |
| ANISOU 24 OH TYR A 2 1632 2220 1284 -243 586 -421 O | |
| ATOM 25 N ASP A 3 19.665 20.306 9.626 1.00 5.27 N | |
| ANISOU 25 N ASP A 3 586 666 749 107 11 2 N | |
| ATOM 26 CA ASP A 3 18.477 20.539 10.432 1.00 5.27 C | |
| ANISOU 26 CA ASP A 3 729 665 608 158 98 -64 C | |
| ATOM 27 C ASP A 3 17.534 19.329 10.398 1.00 4.73 C | |
| ANISOU 27 C ASP A 3 517 722 561 228 19 -18 C | |
| ATOM 28 O ASP A 3 17.294 18.804 9.311 1.00 5.80 O | |
| ANISOU 28 O ASP A 3 894 748 563 23 9 -51 O | |
| ATOM 29 CB ASP A 3 17.779 21.778 9.904 1.00 6.15 C | |
| ANISOU 29 CB ASP A 3 792 596 950 201 73 -131 C | |
| ATOM 30 CG ASP A 3 16.612 22.194 10.723 1.00 6.26 C | |
| ANISOU 30 CG ASP A 3 807 686 886 145 46 -73 C | |
| ATOM 31 OD1 ASP A 3 15.530 21.611 10.650 1.00 7.43 O | |
| ANISOU 31 OD1 ASP A 3 855 729 1239 -35 230 -262 O | |
| ATOM 32 OD2 ASP A 3 16.854 23.197 11.512 1.00 8.48 O | |
| ANISOU 32 OD2 ASP A 3 998 933 1290 179 -54 -517 O | |
| ATOM 33 N PRO A 4 17.026 18.889 11.526 1.00 5.29 N | |
| ANISOU 33 N PRO A 4 749 688 573 57 42 -32 N | |
| ATOM 34 CA PRO A 4 16.223 17.660 11.537 1.00 5.94 C | |
| ANISOU 34 CA PRO A 4 910 578 767 82 75 -31 C | |
| ATOM 35 C PRO A 4 14.852 17.788 10.907 1.00 6.30 C | |
| ANISOU 35 C PRO A 4 692 672 1031 -38 172 57 C | |
| ATOM 36 O PRO A 4 14.260 16.756 10.578 1.00 8.02 O | |
| ANISOU 36 O PRO A 4 874 679 1495 -137 172 -66 O | |
| ATOM 37 CB PRO A 4 16.101 17.319 13.047 1.00 9.97 C | |
| ANISOU 37 CB PRO A 4 1896 1139 755 -475 111 214 C | |
| ATOM 38 CG PRO A 4 16.246 18.639 13.686 1.00 12.06 C | |
| ANISOU 38 CG PRO A 4 2379 1471 731 -718 399 -34 C | |
| ATOM 39 CD PRO A 4 17.243 19.407 12.889 1.00 7.32 C | |
| ANISOU 39 CD PRO A 4 1185 1090 506 -247 67 -115 C | |
| ATOM 40 N GLU A 5 14.331 19.012 10.801 1.00 6.60 N | |
| ANISOU 40 N GLU A 5 829 693 986 99 19 -110 N | |
| ATOM 41 CA GLU A 5 13.040 19.289 10.212 1.00 7.65 C | |
| ANISOU 41 CA GLU A 5 663 949 1296 212 156 10 C | |
| ATOM 42 C GLU A 5 13.132 19.592 8.736 1.00 7.27 C | |
| ANISOU 42 C GLU A 5 585 926 1251 112 -61 -89 C | |
| ATOM 43 O GLU A 5 12.258 19.150 7.953 1.00 10.19 O | |
| ANISOU 43 O GLU A 5 897 1427 1547 -45 -265 -230 O | |
| ATOM 44 CB GLU A 5 12.286 20.421 10.964 1.00 9.50 C | |
| ANISOU 44 CB GLU A 5 1030 1024 1555 287 -43 -347 C | |
| ATOM 45 CG GLU A 5 11.645 19.982 12.241 1.00 18.27 C | |
| ANISOU 45 CG GLU A 5 1652 3412 1879 -101 762 -781 C | |
| ATOM 46 CD GLU A 5 10.495 19.012 12.167 1.00 19.12 C | |
| ANISOU 46 CD GLU A 5 1637 3889 1737 -473 650 -139 C | |
| ATOM 47 OE1 GLU A 5 10.278 18.221 13.127 1.00 30.90 O | |
| ANISOU 47 OE1 GLU A 5 4613 4730 2399 -1474 290 555 O | |
| ATOM 48 OE2 GLU A 5 9.752 19.067 11.167 1.00 28.34 O | |
| ANISOU 48 OE2 GLU A 5 2949 5569 2251 -1216 -282 29 O | |
| ATOM 49 N THR A 6 14.137 20.351 8.314 1.00 7.56 N | |
| ANISOU 49 N THR A 6 763 1147 962 18 -132 29 N | |
| ATOM 50 CA THR A 6 14.200 20.806 6.941 1.00 8.29 C | |
| ANISOU 50 CA THR A 6 1051 1116 983 74 -166 74 C | |
| ATOM 51 C THR A 6 15.255 20.072 6.135 1.00 6.59 C | |
| ANISOU 51 C THR A 6 827 908 771 -50 -269 107 C | |
| ATOM 52 O THR A 6 15.240 20.133 4.900 1.00 8.09 O | |
| ANISOU 52 O THR A 6 1125 1125 824 25 -303 34 O | |
| ATOM 53 CB THR A 6 14.511 22.290 6.824 1.00 10.65 C | |
| ANISOU 53 CB THR A 6 2052 977 1016 402 -142 73 C | |
| ATOM 54 OG1 THR A 6 15.802 22.534 7.368 1.00 11.20 O | |
| ANISOU 54 OG1 THR A 6 2386 840 1028 -267 -159 -94 O | |
| ATOM 55 CG2 THR A 6 13.536 23.152 7.626 1.00 16.54 C | |
| ANISOU 55 CG2 THR A 6 3334 1515 1437 1353 436 353 C | |
| ATOM 56 N GLY A 7 16.216 19.385 6.751 1.00 6.30 N | |
| ANISOU 56 N GLY A 7 907 665 824 -112 -74 172 N | |
| ATOM 57 CA GLY A 7 17.256 18.676 6.039 1.00 5.88 C | |
| ANISOU 57 CA GLY A 7 780 581 874 -199 -150 78 C | |
| ATOM 58 C GLY A 7 18.259 19.556 5.361 1.00 6.51 C | |
| ANISOU 58 C GLY A 7 1048 480 946 -173 30 111 C | |
| ATOM 59 O GLY A 7 19.015 19.091 4.506 1.00 9.78 O | |
| ANISOU 59 O GLY A 7 1166 809 1743 -78 497 29 O | |
| ATOM 60 N THR A 8 18.362 20.804 5.695 1.00 5.98 N | |
| ANISOU 60 N THR A 8 869 662 740 -288 -70 64 N | |
| ATOM 61 CA THR A 8 19.242 21.760 5.125 1.00 5.66 C | |
| ANISOU 61 CA THR A 8 740 585 827 -270 -164 23 C | |
| ATOM 62 C THR A 8 20.419 22.026 6.074 1.00 5.15 C | |
| ANISOU 62 C THR A 8 842 528 588 -262 -107 61 C | |
| ATOM 63 O THR A 8 20.317 21.872 7.313 1.00 6.36 O | |
| ANISOU 63 O THR A 8 818 962 635 -73 -91 169 O | |
| ATOM 64 CB THR A 8 18.553 23.073 4.762 1.00 9.09 C | |
| ANISOU 64 CB THR A 8 1397 762 1294 -179 -578 207 C | |
| ATOM 65 OG1 THR A 8 17.905 23.602 5.922 1.00 10.05 O | |
| ANISOU 65 OG1 THR A 8 1164 832 1823 216 -488 29 O | |
| ATOM 66 CG2 THR A 8 17.498 22.871 3.686 1.00 11.85 C | |
| ANISOU 66 CG2 THR A 8 1277 1603 1622 -427 -774 589 C | |
| ATOM 67 N TRP A 9 21.517 22.418 5.517 1.00 5.75 N | |
| ANISOU 67 N TRP A 9 823 805 556 -342 -145 82 N | |
| ATOM 68 CA TRP A 9 22.762 22.680 6.241 1.00 4.78 C | |
| ANISOU 68 CA TRP A 9 723 538 556 -74 0 6 C | |
| ATOM 69 C TRP A 9 22.687 24.060 6.869 1.00 4.96 C | |
| ANISOU 69 C TRP A 9 741 511 633 -196 -14 91 C | |
| ATOM 70 O TRP A 9 22.321 25.031 6.185 1.00 7.83 O | |
| ANISOU 70 O TRP A 9 1496 595 884 -23 -365 87 O | |
| ATOM 71 CB TRP A 9 23.924 22.604 5.307 1.00 6.90 C | |
| ANISOU 71 CB TRP A 9 781 955 884 -94 110 -69 C | |
| ATOM 72 CG TRP A 9 25.267 22.745 5.969 1.00 6.58 C | |
| ANISOU 72 CG TRP A 9 696 878 927 -120 153 -7 C | |
| ATOM 73 CD1 TRP A 9 26.024 23.847 6.060 1.00 9.48 C | |
| ANISOU 73 CD1 TRP A 9 873 1071 1659 -309 29 207 C | |
| ATOM 74 CD2 TRP A 9 25.975 21.701 6.641 1.00 6.96 C | |
| ANISOU 74 CD2 TRP A 9 714 994 939 -138 82 19 C | |
| ATOM 75 NE1 TRP A 9 27.180 23.571 6.750 1.00 10.18 N | |
| ANISOU 75 NE1 TRP A 9 736 1373 1759 -438 54 121 N | |
| ATOM 76 CE2 TRP A 9 27.178 22.245 7.100 1.00 7.80 C | |
| ANISOU 76 CE2 TRP A 9 657 1347 958 -292 75 32 C | |
| ATOM 77 CE3 TRP A 9 25.747 20.347 6.894 1.00 8.84 C | |
| ANISOU 77 CE3 TRP A 9 1082 818 1458 -23 -255 -197 C | |
| ATOM 78 CZ2 TRP A 9 28.125 21.492 7.781 1.00 10.37 C | |
| ANISOU 78 CZ2 TRP A 9 741 1704 1497 -42 -51 -16 C | |
| ATOM 79 CZ3 TRP A 9 26.676 19.593 7.572 1.00 10.97 C | |
| ANISOU 79 CZ3 TRP A 9 1153 961 2054 226 -206 -128 C | |
| ATOM 80 CH2 TRP A 9 27.865 20.176 8.026 1.00 10.75 C | |
| ANISOU 80 CH2 TRP A 9 1020 1424 1639 362 -201 -352 C | |
| ATOM 81 N TYR A 10 23.053 24.188 8.139 1.00 5.32 N | |
| ANISOU 81 N TYR A 10 835 603 582 -111 -48 41 N | |
| ATOM 82 CA TYR A 10 23.135 25.467 8.794 1.00 5.77 C | |
| ANISOU 82 CA TYR A 10 999 524 669 -145 -87 15 C | |
| ATOM 83 C TYR A 10 24.386 25.590 9.646 1.00 6.26 C | |
| ANISOU 83 C TYR A 10 921 621 836 -235 59 -128 C | |
| ATOM 84 O TYR A 10 24.585 26.750 10.070 1.00 7.80 O | |
| ANISOU 84 O TYR A 10 1092 746 1127 -334 -65 -227 O | |
| ATOM 85 CB TYR A 10 21.862 25.753 9.636 1.00 6.56 C | |
| ANISOU 85 CB TYR A 10 931 682 881 50 -102 -115 C | |
| ATOM 86 CG TYR A 10 21.754 24.860 10.821 1.00 5.72 C | |
| ANISOU 86 CG TYR A 10 671 779 724 -17 43 -163 C | |
| ATOM 87 CD1 TYR A 10 22.199 25.208 12.100 1.00 8.96 C | |
| ANISOU 87 CD1 TYR A 10 1759 892 754 -331 26 -249 C | |
| ATOM 88 CD2 TYR A 10 21.203 23.586 10.716 1.00 6.13 C | |
| ANISOU 88 CD2 TYR A 10 731 986 613 -201 -156 -59 C | |
| ATOM 89 CE1 TYR A 10 22.104 24.385 13.182 1.00 9.28 C | |
| ANISOU 89 CE1 TYR A 10 1838 1128 561 -437 -39 -241 C | |
| ATOM 90 CE2 TYR A 10 21.118 22.747 11.804 1.00 6.42 C | |
| ANISOU 90 CE2 TYR A 10 663 1137 641 -363 28 -79 C | |
| ATOM 91 CZ TYR A 10 21.563 23.125 13.050 1.00 6.27 C | |
| ANISOU 91 CZ TYR A 10 873 1043 467 -108 140 -106 C | |
| ATOM 92 OH TYR A 10 21.499 22.315 14.128 1.00 8.82 O | |
| ANISOU 92 OH TYR A 10 1457 1357 535 -467 60 -104 O | |
| ATOM 93 OXT TYR A 10 25.084 24.587 9.884 1.00 6.99 O | |
| ANISOU 93 OXT TYR A 10 773 860 1023 -125 -204 -150 O | |
| TER 94 TYR A 10 | |
| HETATM 95 O HOH A 101 7.813 17.749 10.939 1.00 33.46 O | |
| ANISOU 95 O HOH A 101 2429 2631 7653 759 -165 -320 O | |
| HETATM 96 O HOH A 102 30.527 20.889 16.186 1.00 34.87 O | |
| ANISOU 96 O HOH A 102 2466 6021 4761 931 -1857 -2131 O | |
| HETATM 97 O HOH A 103 20.817 19.783 13.738 1.00 10.24 O | |
| ANISOU 97 O HOH A 103 1786 1261 842 -553 -100 134 O | |
| HETATM 98 O HOH A 104 19.706 25.504 6.460 1.00 25.64 O | |
| ANISOU 98 O HOH A 104 2301 2218 5224 1073 -1856 -1239 O | |
| HETATM 99 O HOH A 105 19.246 16.798 3.137 0.50 21.96 O | |
| ANISOU 99 O HOH A 105 3268 3354 1720 1549 0 0 O | |
| HETATM 100 O HOH A 106 13.782 21.392 2.921 1.00 14.09 O | |
| ANISOU 100 O HOH A 106 1634 1443 2276 -166 -738 296 O | |
| HETATM 101 O HOH A 107 27.076 15.685 3.844 1.00 33.07 O | |
| ANISOU 101 O HOH A 107 3453 5461 3650 1924 763 -338 O | |
| HETATM 102 O HOH A 108 28.383 22.298 11.296 1.00 18.18 O | |
| ANISOU 102 O HOH A 108 1022 3711 2175 44 -118 -162 O | |
| HETATM 103 O HOH A 109 29.871 24.582 7.637 1.00 68.49 O | |
| ANISOU 103 O HOH A 109 9275 7095 9654 1983 -458 1020 O | |
| HETATM 104 O HOH A 110 18.361 25.585 12.710 1.00 17.73 O | |
| ANISOU 104 O HOH A 110 1576 1757 3404 -298 791 -169 O | |
| HETATM 105 O HOH A 111 8.897 16.529 8.446 0.50 24.45 O | |
| ANISOU 105 O HOH A 111 3279 768 5243 -397 -974 601 O | |
| HETATM 106 O HOH A 112 9.623 16.798 5.908 0.50 64.33 O | |
| ANISOU 106 O HOH A 112 8243 8592 7607 788 0 0 O | |
| MASTER 228 0 0 0 0 0 0 6 105 1 0 1 | |
| END | |