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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
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