allpy: 0c3c1856113a test/1kfm.pdb

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view test/1kfm.pdb @ 309:0c3c1856113a

Moved base.Blog.geometrical_cores to pdb.Block

author	Daniil Alexeyevsky <me.dendik@gmail.com>
date	Thu, 16 Dec 2010 20:47:09 +0300
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1 HEADER MEMBRANE PROTEIN 21-NOV-01 1KFM

2 TITLE CORE SIDE-CHAIN PACKING AND BACKBONE CONFORMATION IN LPP-56

3 TITLE 2 COILED-COIL MUTANTS

4 COMPND MOL_ID: 1;

5 COMPND 2 MOLECULE: MAJOR OUTER MEMBRANE LIPOPROTEIN;

6 COMPND 3 CHAIN: A;

7 COMPND 4 SYNONYM: MUREIN-LIPOPROTEIN LPP, MUREIN-LIPOPROTEIN LPP;

8 COMPND 5 ENGINEERED: YES;

9 COMPND 6 MUTATION: YES

10 SOURCE MOL_ID: 1;

11 SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;

12 SOURCE 3 ORGANISM_TAXID: 562;

13 SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;

14 SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562;

15 SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID

16 KEYWDS LIPOPROTEIN, PROTEIN FOLDING, COILED COIL, HELIX CAPPING,

17 KEYWDS 2 ALANINE-ZIPPER, MEMBRANE PROTEIN

18 EXPDTA X-RAY DIFFRACTION

19 AUTHOR J.LIU,W.CAO,M.LU

20 REVDAT 2 24-FEB-09 1KFM 1 VERSN

21 REVDAT 1 28-JUN-02 1KFM 0

22 JRNL AUTH J.LIU,W.CAO,M.LU

23 JRNL TITL CORE SIDE-CHAIN PACKING AND BACKBONE CONFORMATION

24 JRNL TITL 2 IN LPP-56 COILED-COIL MUTANTS.

25 JRNL REF J.MOL.BIOL. V. 318 877 2002

26 JRNL REFN ISSN 0022-2836

27 JRNL PMID 12054830

28 JRNL DOI 10.1016/S0022-2836(02)00138-9

29 REMARK 1

30 REMARK 2

31 REMARK 2 RESOLUTION. 2.00 ANGSTROMS.

32 REMARK 3

33 REMARK 3 REFINEMENT.

34 REMARK 3 PROGRAM : CNS 1.0

35 REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-

36 REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU,

37 REMARK 3 : READ,RICE,SIMONSON,WARREN

38 REMARK 3

39 REMARK 3 REFINEMENT TARGET : ENGH & HUBER

40 REMARK 3

41 REMARK 3 DATA USED IN REFINEMENT.

42 REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00

43 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 25.26

44 REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000

45 REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL

46 REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL

47 REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 97.8

48 REMARK 3 NUMBER OF REFLECTIONS : 2761

49 REMARK 3

50 REMARK 3 FIT TO DATA USED IN REFINEMENT.

51 REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT

52 REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM

53 REMARK 3 R VALUE (WORKING SET) : 0.260

54 REMARK 3 FREE R VALUE : 0.288

55 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 9.200

56 REMARK 3 FREE R VALUE TEST SET COUNT : 254

57 REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.018

58 REMARK 3

59 REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.

60 REMARK 3 TOTAL NUMBER OF BINS USED : 10

61 REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.00

62 REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.07

63 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 97.00

64 REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 267

65 REMARK 3 BIN R VALUE (WORKING SET) : 0.3530

66 REMARK 3 BIN FREE R VALUE : 0.3560

67 REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 9.00

68 REMARK 3 BIN FREE R VALUE TEST SET COUNT : 25

69 REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.074

70 REMARK 3

71 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.

72 REMARK 3 PROTEIN ATOMS : 363

73 REMARK 3 NUCLEIC ACID ATOMS : 0

74 REMARK 3 HETEROGEN ATOMS : 0

75 REMARK 3 SOLVENT ATOMS : 19

76 REMARK 3

77 REMARK 3 B VALUES.

78 REMARK 3 FROM WILSON PLOT (A**2) : 39.00

79 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 43.60

80 REMARK 3 OVERALL ANISOTROPIC B VALUE.

81 REMARK 3 B11 (A**2) : 1.61000

82 REMARK 3 B22 (A**2) : 1.61000

83 REMARK 3 B33 (A**2) : -3.21000

84 REMARK 3 B12 (A**2) : 4.24000

85 REMARK 3 B13 (A**2) : 0.00000

86 REMARK 3 B23 (A**2) : 0.00000

87 REMARK 3

88 REMARK 3 ESTIMATED COORDINATE ERROR.

89 REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.29

90 REMARK 3 ESD FROM SIGMAA (A) : 0.21

91 REMARK 3 LOW RESOLUTION CUTOFF (A) : 5.00

92 REMARK 3

93 REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.

94 REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.31

95 REMARK 3 ESD FROM C-V SIGMAA (A) : 0.24

96 REMARK 3

97 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.

98 REMARK 3 BOND LENGTHS (A) : 0.004

99 REMARK 3 BOND ANGLES (DEGREES) : 0.90

100 REMARK 3 DIHEDRAL ANGLES (DEGREES) : 16.10

101 REMARK 3 IMPROPER ANGLES (DEGREES) : 0.63

102 REMARK 3

103 REMARK 3 ISOTROPIC THERMAL MODEL : RESTRAINED

104 REMARK 3

105 REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA

106 REMARK 3 MAIN-CHAIN BOND (A**2) : 1.510 ; 1.500

107 REMARK 3 MAIN-CHAIN ANGLE (A**2) : 2.380 ; 2.000

108 REMARK 3 SIDE-CHAIN BOND (A**2) : 2.660 ; 2.000

109 REMARK 3 SIDE-CHAIN ANGLE (A**2) : 4.170 ; 2.500

110 REMARK 3

111 REMARK 3 BULK SOLVENT MODELING.

112 REMARK 3 METHOD USED : FLAT MODEL

113 REMARK 3 KSOL : 0.43

114 REMARK 3 BSOL : 62.15

115 REMARK 3

116 REMARK 3 NCS MODEL : NULL

117 REMARK 3

118 REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT

119 REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL

120 REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL

121 REMARK 3

122 REMARK 3 PARAMETER FILE 1 : PROTEIN_REP.PARAM

123 REMARK 3 PARAMETER FILE 2 : WATER_REP.PARAM

124 REMARK 3 PARAMETER FILE 3 : NULL

125 REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP

126 REMARK 3 TOPOLOGY FILE 2 : WATER.TOP

127 REMARK 3 TOPOLOGY FILE 3 : NULL

128 REMARK 3

129 REMARK 3 OTHER REFINEMENT REMARKS: NULL

130 REMARK 4

131 REMARK 4 1KFM COMPLIES WITH FORMAT V. 3.15, 01-DEC-08

132 REMARK 100

133 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 03-DEC-01.

134 REMARK 100 THE RCSB ID CODE IS RCSB014904.

135 REMARK 200

136 REMARK 200 EXPERIMENTAL DETAILS

137 REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION

138 REMARK 200 DATE OF DATA COLLECTION : 12-OCT-01

139 REMARK 200 TEMPERATURE (KELVIN) : 95

140 REMARK 200 PH : 6.8

141 REMARK 200 NUMBER OF CRYSTALS USED : 1

142 REMARK 200

143 REMARK 200 SYNCHROTRON (Y/N) : Y

144 REMARK 200 RADIATION SOURCE : NSLS

145 REMARK 200 BEAMLINE : X25

146 REMARK 200 X-RAY GENERATOR MODEL : NULL

147 REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M

148 REMARK 200 WAVELENGTH OR RANGE (A) : 1.1000

149 REMARK 200 MONOCHROMATOR : GRAPHITE

150 REMARK 200 OPTICS : NULL

151 REMARK 200

152 REMARK 200 DETECTOR TYPE : CCD

153 REMARK 200 DETECTOR MANUFACTURER : BRANDEIS - B4

154 REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MADNES

155 REMARK 200 DATA SCALING SOFTWARE : SCALEPACK

156 REMARK 200

157 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 2761

158 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000

159 REMARK 200 RESOLUTION RANGE LOW (A) : 50.000

160 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000

161 REMARK 200

162 REMARK 200 OVERALL.

163 REMARK 200 COMPLETENESS FOR RANGE (%) : 97.8

164 REMARK 200 DATA REDUNDANCY : 3.800

165 REMARK 200 R MERGE (I) : 0.04200

166 REMARK 200 R SYM (I) : NULL

167 REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 17.5000

168 REMARK 200

169 REMARK 200 IN THE HIGHEST RESOLUTION SHELL.

170 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00

171 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.07

172 REMARK 200 COMPLETENESS FOR SHELL (%) : 97.0

173 REMARK 200 DATA REDUNDANCY IN SHELL : 3.90

174 REMARK 200 R MERGE FOR SHELL (I) : 0.09700

175 REMARK 200 R SYM FOR SHELL (I) : NULL

176 REMARK 200 <I/SIGMA(I)> FOR SHELL : 12.300

177 REMARK 200

178 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH

179 REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT

180 REMARK 200 SOFTWARE USED: AMORE

181 REMARK 200 STARTING MODEL: PDB ENTRY 1EQ7

182 REMARK 200

183 REMARK 200 REMARK: NULL

184 REMARK 280

185 REMARK 280 CRYSTAL

186 REMARK 280 SOLVENT CONTENT, VS (%): NULL

187 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): NULL

188 REMARK 280

189 REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 4000, SODIUM CACODYLATE,

190 REMARK 280 AMMONIUM ACETATE, PH 6.8, VAPOR DIFFUSION, HANGING DROP AT

191 REMARK 280 293K, VAPOR DIFFUSION, HANGING DROP

192 REMARK 290

193 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY

194 REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: H 3

195 REMARK 290

196 REMARK 290 SYMOP SYMMETRY

197 REMARK 290 NNNMMM OPERATOR

198 REMARK 290 1555 X,Y,Z

199 REMARK 290 2555 -Y,X-Y,Z

200 REMARK 290 3555 -X+Y,-X,Z

201 REMARK 290 4555 X+2/3,Y+1/3,Z+1/3

202 REMARK 290 5555 -Y+2/3,X-Y+1/3,Z+1/3

203 REMARK 290 6555 -X+Y+2/3,-X+1/3,Z+1/3

204 REMARK 290 7555 X+1/3,Y+2/3,Z+2/3

205 REMARK 290 8555 -Y+1/3,X-Y+2/3,Z+2/3

206 REMARK 290 9555 -X+Y+1/3,-X+2/3,Z+2/3

207 REMARK 290

208 REMARK 290 WHERE NNN -> OPERATOR NUMBER

209 REMARK 290 MMM -> TRANSLATION VECTOR

210 REMARK 290

211 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS

212 REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM

213 REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY

214 REMARK 290 RELATED MOLECULES.

215 REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000

216 REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000

217 REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000

218 REMARK 290 SMTRY1 2 -0.500000 -0.866025 0.000000 0.00000

219 REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000

220 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000

221 REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000

222 REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000

223 REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000

224 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 18.52850

225 REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 10.69743

226 REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 27.30400

227 REMARK 290 SMTRY1 5 -0.500000 -0.866025 0.000000 18.52850

228 REMARK 290 SMTRY2 5 0.866025 -0.500000 0.000000 10.69743

229 REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 27.30400

230 REMARK 290 SMTRY1 6 -0.500000 0.866025 0.000000 18.52850

231 REMARK 290 SMTRY2 6 -0.866025 -0.500000 0.000000 10.69743

232 REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 27.30400

233 REMARK 290 SMTRY1 7 1.000000 0.000000 0.000000 0.00000

234 REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 21.39487

235 REMARK 290 SMTRY3 7 0.000000 0.000000 1.000000 54.60800

236 REMARK 290 SMTRY1 8 -0.500000 -0.866025 0.000000 0.00000

237 REMARK 290 SMTRY2 8 0.866025 -0.500000 0.000000 21.39487

238 REMARK 290 SMTRY3 8 0.000000 0.000000 1.000000 54.60800

239 REMARK 290 SMTRY1 9 -0.500000 0.866025 0.000000 0.00000

240 REMARK 290 SMTRY2 9 -0.866025 -0.500000 0.000000 21.39487

241 REMARK 290 SMTRY3 9 0.000000 0.000000 1.000000 54.60800

242 REMARK 290

243 REMARK 290 REMARK: NULL

244 REMARK 300

245 REMARK 300 BIOMOLECULE: 1

246 REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM

247 REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN

248 REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON

249 REMARK 300 BURIED SURFACE AREA.

250 REMARK 300 REMARK: THE BIOLOGICAL ASSEMBLY IS A TRIMER GENERATED FROM THE

251 REMARK 300 MONOMER BY THE THREE FOLD AXIS.

252 REMARK 350

253 REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN

254 REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE

255 REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS

256 REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND

257 REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.

258 REMARK 350

259 REMARK 350 BIOMOLECULE: 1

260 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC

261 REMARK 350 APPLY THE FOLLOWING TO CHAINS: A

262 REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000

263 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000

264 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000

265 REMARK 350 BIOMT1 2 -0.500000 -0.866025 0.000000 55.58550

266 REMARK 350 BIOMT2 2 0.866025 -0.500000 0.000000 -32.09230

267 REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 0.00000

268 REMARK 350 BIOMT1 3 -0.500000 0.866025 0.000000 55.58550

269 REMARK 350 BIOMT2 3 -0.866025 -0.500000 0.000000 32.09230

270 REMARK 350 BIOMT3 3 0.000000 0.000000 1.000000 0.00000

271 REMARK 465

272 REMARK 465 MISSING RESIDUES

273 REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE

274 REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN

275 REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)

276 REMARK 465

277 REMARK 465 M RES C SSSEQI

278 REMARK 465 SER A 1

279 REMARK 465 ALA A 52

280 REMARK 465 THR A 53

281 REMARK 465 LYS A 54

282 REMARK 465 TYR A 55

283 REMARK 465 ARG A 56

284 REMARK 470

285 REMARK 470 MISSING ATOM

286 REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS(M=MODEL NUMBER;

287 REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;

288 REMARK 470 I=INSERTION CODE):

289 REMARK 470 M RES CSSEQI ATOMS

290 REMARK 470 ASN A 3 CG OD1 ND2

291 REMARK 470 ASP A 12 CG OD1 OD2

292 REMARK 470 GLN A 14 CG CD OE1 NE2

293 REMARK 900

294 REMARK 900 RELATED ENTRIES

295 REMARK 900 RELATED ID: 1EQ7 RELATED DB: PDB

296 REMARK 900 THE WILD TYPE PROTEIN STRUCTURE

297 REMARK 900 RELATED ID: 1JCB RELATED DB: PDB

298 REMARK 900 THE STRUCTURE OF THE SAME SEQUENCE REFINED AT A LOWER

299 REMARK 900 SOLUTION

300 REMARK 900 RELATED ID: 1KFN RELATED DB: PDB

301 REMARK 900 MUTANT OF 1EQ7

302 DBREF 1KFM A 1 56 UNP P69776 LPP_ECOLI 22 77

303 SEQADV 1KFM ALA A 30 UNP P69776 MET 51 ENGINEERED

304 SEQADV 1KFM ALA A 34 UNP P69776 VAL 55 ENGINEERED

305 SEQRES 1 A 56 SER SER ASN ALA LYS ILE ASP GLN LEU SER SER ASP VAL

306 SEQRES 2 A 56 GLN THR LEU ASN ALA LYS VAL ASP GLN LEU SER ASN ASP

307 SEQRES 3 A 56 VAL ASN ALA ALA ARG SER ASP ALA GLN ALA ALA LYS ASP

308 SEQRES 4 A 56 ASP ALA ALA ARG ALA ASN GLN ARG LEU ASP ASN MET ALA

309 SEQRES 5 A 56 THR LYS TYR ARG

310 FORMUL 2 HOH *19(H2 O)

311 HELIX 1 1 SER A 2 ASN A 50 1 49

312 CRYST1 37.057 37.057 81.912 90.00 90.00 120.00 H 3 9

313 ORIGX1 1.000000 0.000000 0.000000 0.00000

314 ORIGX2 0.000000 1.000000 0.000000 0.00000

315 ORIGX3 0.000000 0.000000 1.000000 0.00000

316 SCALE1 0.026985 0.015580 0.000000 0.00000

317 SCALE2 0.000000 0.031160 0.000000 0.00000

318 SCALE3 0.000000 0.000000 0.012208 0.00000

319 ATOM 1 N SER A 2 42.312 3.607 38.680 1.00 60.07 N

320 ATOM 2 CA SER A 2 41.475 2.912 37.661 1.00 59.34 C

321 ATOM 3 C SER A 2 40.549 3.869 36.903 1.00 58.86 C

322 ATOM 4 O SER A 2 40.011 3.520 35.855 1.00 58.04 O

323 ATOM 5 CB SER A 2 40.648 1.807 38.332 1.00 60.00 C

324 ATOM 6 OG SER A 2 40.103 2.244 39.570 1.00 60.97 O

325 ATOM 7 N ASN A 3 40.372 5.078 37.425 1.00 58.19 N

326 ATOM 8 CA ASN A 3 39.503 6.057 36.777 1.00 56.34 C

327 ATOM 9 C ASN A 3 40.091 6.553 35.456 1.00 55.52 C

328 ATOM 10 O ASN A 3 39.397 6.612 34.437 1.00 53.57 O

329 ATOM 11 CB ASN A 3 39.260 7.246 37.711 1.00 57.41 C

330 ATOM 12 N ALA A 4 41.372 6.909 35.481 1.00 54.17 N

331 ATOM 13 CA ALA A 4 42.051 7.410 34.292 1.00 53.88 C

332 ATOM 14 C ALA A 4 42.139 6.342 33.204 1.00 53.23 C

333 ATOM 15 O ALA A 4 41.975 6.635 32.021 1.00 52.43 O

334 ATOM 16 CB ALA A 4 43.438 7.900 34.660 1.00 53.56 C

335 ATOM 17 N LYS A 5 42.394 5.103 33.616 1.00 53.13 N

336 ATOM 18 CA LYS A 5 42.499 3.979 32.690 1.00 51.43 C

337 ATOM 19 C LYS A 5 41.230 3.850 31.848 1.00 50.61 C

338 ATOM 20 O LYS A 5 41.291 3.637 30.637 1.00 50.14 O

339 ATOM 21 CB LYS A 5 42.716 2.683 33.473 1.00 54.37 C

340 ATOM 22 CG LYS A 5 42.792 1.440 32.606 1.00 56.77 C

341 ATOM 23 CD LYS A 5 44.144 1.311 31.921 1.00 58.93 C

342 ATOM 24 CE LYS A 5 45.227 0.946 32.922 1.00 59.76 C

343 ATOM 25 NZ LYS A 5 46.520 0.641 32.259 1.00 61.61 N

344 ATOM 26 N ILE A 6 40.082 3.985 32.502 1.00 48.29 N

345 ATOM 27 CA ILE A 6 38.789 3.871 31.841 1.00 46.88 C

346 ATOM 28 C ILE A 6 38.462 5.063 30.940 1.00 46.99 C

347 ATOM 29 O ILE A 6 37.828 4.913 29.892 1.00 44.24 O

348 ATOM 30 CB ILE A 6 37.668 3.710 32.883 1.00 47.74 C

349 ATOM 31 CG1 ILE A 6 37.943 2.468 33.735 1.00 49.74 C

350 ATOM 32 CG2 ILE A 6 36.317 3.610 32.195 1.00 48.53 C

351 ATOM 33 CD1 ILE A 6 36.891 2.194 34.792 1.00 51.05 C

352 ATOM 34 N ASP A 7 38.881 6.255 31.339 1.00 47.06 N

353 ATOM 35 CA ASP A 7 38.592 7.404 30.504 1.00 48.63 C

354 ATOM 36 C ASP A 7 39.556 7.484 29.328 1.00 46.66 C

355 ATOM 37 O ASP A 7 39.320 8.223 28.375 1.00 47.36 O

356 ATOM 38 CB ASP A 7 38.589 8.681 31.338 1.00 51.70 C

357 ATOM 39 CG ASP A 7 37.365 8.773 32.232 1.00 53.80 C

358 ATOM 40 OD1 ASP A 7 36.232 8.751 31.700 1.00 55.73 O

359 ATOM 41 OD2 ASP A 7 37.530 8.859 33.465 1.00 57.34 O

360 ATOM 42 N GLN A 8 40.638 6.712 29.389 1.00 46.13 N

361 ATOM 43 CA GLN A 8 41.586 6.672 28.280 1.00 45.21 C

362 ATOM 44 C GLN A 8 40.928 5.727 27.273 1.00 43.76 C

363 ATOM 45 O GLN A 8 41.036 5.894 26.056 1.00 40.68 O

364 ATOM 46 CB GLN A 8 42.932 6.094 28.722 1.00 48.47 C

365 ATOM 47 CG GLN A 8 43.947 5.965 27.594 1.00 51.00 C

366 ATOM 48 CD GLN A 8 44.616 7.283 27.238 1.00 55.95 C

367 ATOM 49 OE1 GLN A 8 43.949 8.283 26.962 1.00 58.34 O

368 ATOM 50 NE2 GLN A 8 45.944 7.287 27.237 1.00 55.76 N

369 ATOM 51 N LEU A 9 40.237 4.727 27.803 1.00 41.22 N

370 ATOM 52 CA LEU A 9 39.536 3.763 26.967 1.00 42.16 C

371 ATOM 53 C LEU A 9 38.336 4.440 26.320 1.00 40.27 C

372 ATOM 54 O LEU A 9 38.118 4.297 25.124 1.00 37.87 O

373 ATOM 55 CB LEU A 9 39.070 2.574 27.801 1.00 43.31 C

374 ATOM 56 CG LEU A 9 40.186 1.733 28.418 1.00 46.66 C

375 ATOM 57 CD1 LEU A 9 39.580 0.604 29.242 1.00 47.87 C

376 ATOM 58 CD2 LEU A 9 41.073 1.184 27.313 1.00 48.08 C

377 ATOM 59 N SER A 10 37.561 5.172 27.118 1.00 41.39 N

378 ATOM 60 CA SER A 10 36.387 5.880 26.612 1.00 42.69 C

379 ATOM 61 C SER A 10 36.785 6.718 25.406 1.00 42.80 C

380 ATOM 62 O SER A 10 36.114 6.692 24.377 1.00 42.68 O

381 ATOM 63 CB SER A 10 35.799 6.795 27.689 1.00 42.81 C

382 ATOM 64 OG SER A 10 35.291 6.049 28.780 1.00 48.23 O

383 ATOM 65 N SER A 11 37.886 7.454 25.548 1.00 43.67 N

384 ATOM 66 CA SER A 11 38.411 8.301 24.485 1.00 44.33 C

385 ATOM 67 C SER A 11 38.813 7.464 23.279 1.00 43.58 C

386 ATOM 68 O SER A 11 38.421 7.767 22.158 1.00 44.57 O

387 ATOM 69 CB SER A 11 39.635 9.084 24.978 1.00 46.35 C

388 ATOM 70 OG SER A 11 39.308 9.956 26.047 1.00 50.42 O

389 ATOM 71 N ASP A 12 39.602 6.417 23.514 1.00 40.75 N

390 ATOM 72 CA ASP A 12 40.054 5.544 22.442 1.00 40.59 C

391 ATOM 73 C ASP A 12 38.878 5.010 21.637 1.00 41.09 C

392 ATOM 74 O ASP A 12 38.903 5.035 20.408 1.00 41.15 O

393 ATOM 75 CB ASP A 12 40.857 4.369 23.007 1.00 42.94 C

394 ATOM 76 N VAL A 13 37.854 4.528 22.335 1.00 39.47 N

395 ATOM 77 CA VAL A 13 36.668 3.993 21.676 1.00 39.43 C

396 ATOM 78 C VAL A 13 35.957 5.089 20.880 1.00 41.30 C

397 ATOM 79 O VAL A 13 35.424 4.829 19.804 1.00 40.94 O

398 ATOM 80 CB VAL A 13 35.674 3.396 22.702 1.00 39.55 C

399 ATOM 81 CG1 VAL A 13 34.372 2.997 22.003 1.00 39.08 C

400 ATOM 82 CG2 VAL A 13 36.296 2.189 23.389 1.00 36.36 C

401 ATOM 83 N GLN A 14 35.944 6.309 21.416 1.00 41.58 N

402 ATOM 84 CA GLN A 14 35.299 7.429 20.733 1.00 44.48 C

403 ATOM 85 C GLN A 14 36.023 7.726 19.424 1.00 44.95 C

404 ATOM 86 O GLN A 14 35.392 7.923 18.385 1.00 45.35 O

405 ATOM 87 CB GLN A 14 35.317 8.679 21.616 1.00 45.35 C

406 ATOM 88 N THR A 15 37.350 7.759 19.494 1.00 44.62 N

407 ATOM 89 CA THR A 15 38.195 8.019 18.334 1.00 46.25 C

408 ATOM 90 C THR A 15 38.013 6.932 17.284 1.00 45.71 C

409 ATOM 91 O THR A 15 37.876 7.218 16.097 1.00 44.89 O

410 ATOM 92 CB THR A 15 39.684 8.063 18.734 1.00 46.52 C

411 ATOM 93 OG1 THR A 15 39.923 9.210 19.556 1.00 49.82 O

412 ATOM 94 CG2 THR A 15 40.575 8.123 17.501 1.00 49.17 C

413 ATOM 95 N LEU A 16 38.023 5.681 17.730 1.00 45.76 N

414 ATOM 96 CA LEU A 16 37.851 4.553 16.829 1.00 45.55 C

415 ATOM 97 C LEU A 16 36.506 4.642 16.117 1.00 44.75 C

416 ATOM 98 O LEU A 16 36.411 4.381 14.918 1.00 44.17 O

417 ATOM 99 CB LEU A 16 37.947 3.240 17.608 1.00 44.90 C

418 ATOM 100 CG LEU A 16 39.320 2.982 18.232 1.00 46.75 C

419 ATOM 101 CD1 LEU A 16 39.282 1.708 19.071 1.00 45.27 C

420 ATOM 102 CD2 LEU A 16 40.364 2.875 17.128 1.00 47.83 C

421 ATOM 103 N ASN A 17 35.472 5.017 16.861 1.00 44.17 N

422 ATOM 104 CA ASN A 17 34.132 5.145 16.305 1.00 45.86 C

423 ATOM 105 C ASN A 17 34.140 6.118 15.127 1.00 45.47 C

424 ATOM 106 O ASN A 17 33.590 5.827 14.069 1.00 44.04 O

425 ATOM 107 CB ASN A 17 33.163 5.620 17.391 1.00 47.57 C

426 ATOM 108 CG ASN A 17 32.125 4.569 17.744 1.00 51.15 C

427 ATOM 109 OD1 ASN A 17 31.226 4.278 16.955 1.00 52.49 O

428 ATOM 110 ND2 ASN A 17 32.251 3.989 18.930 1.00 52.38 N

429 ATOM 111 N ALA A 18 34.787 7.262 15.316 1.00 44.71 N

430 ATOM 112 CA ALA A 18 34.886 8.276 14.277 1.00 45.40 C

431 ATOM 113 C ALA A 18 35.663 7.738 13.079 1.00 45.45 C

432 ATOM 114 O ALA A 18 35.343 8.046 11.931 1.00 44.74 O

433 ATOM 115 CB ALA A 18 35.575 9.522 14.834 1.00 45.73 C

434 ATOM 116 N LYS A 19 36.683 6.931 13.347 1.00 46.31 N

435 ATOM 117 CA LYS A 19 37.493 6.361 12.279 1.00 47.51 C

436 ATOM 118 C LYS A 19 36.738 5.310 11.484 1.00 47.31 C

437 ATOM 119 O LYS A 19 36.917 5.191 10.274 1.00 46.23 O

438 ATOM 120 CB LYS A 19 38.768 5.730 12.840 1.00 47.96 C

439 ATOM 121 CG LYS A 19 39.934 6.693 12.979 1.00 50.40 C

440 ATOM 122 CD LYS A 19 41.240 5.945 13.205 1.00 52.41 C

441 ATOM 123 CE LYS A 19 41.520 4.961 12.077 1.00 54.42 C

442 ATOM 124 NZ LYS A 19 41.508 5.614 10.736 1.00 56.90 N

443 ATOM 125 N VAL A 20 35.904 4.537 12.169 1.00 47.77 N

444 ATOM 126 CA VAL A 20 35.139 3.496 11.503 1.00 48.20 C

445 ATOM 127 C VAL A 20 33.965 4.070 10.710 1.00 49.23 C

446 ATOM 128 O VAL A 20 33.608 3.538 9.662 1.00 50.16 O

447 ATOM 129 CB VAL A 20 34.624 2.453 12.515 1.00 48.43 C

448 ATOM 130 CG1 VAL A 20 33.819 1.385 11.796 1.00 47.98 C

449 ATOM 131 CG2 VAL A 20 35.803 1.807 13.235 1.00 47.79 C

450 ATOM 132 N ASP A 21 33.365 5.149 11.202 1.00 49.97 N

451 ATOM 133 CA ASP A 21 32.246 5.768 10.490 1.00 52.04 C

452 ATOM 134 C ASP A 21 32.723 6.359 9.172 1.00 51.81 C

453 ATOM 135 O ASP A 21 32.095 6.172 8.130 1.00 52.11 O

454 ATOM 136 CB ASP A 21 31.603 6.887 11.314 1.00 53.33 C

455 ATOM 137 CG ASP A 21 30.743 6.366 12.445 1.00 53.82 C

456 ATOM 138 OD1 ASP A 21 30.223 5.234 12.328 1.00 56.51 O

457 ATOM 139 OD2 ASP A 21 30.573 7.101 13.443 1.00 53.35 O

458 ATOM 140 N GLN A 22 33.835 7.082 9.227 1.00 51.30 N

459 ATOM 141 CA GLN A 22 34.384 7.702 8.033 1.00 50.82 C

460 ATOM 142 C GLN A 22 34.934 6.675 7.049 1.00 48.21 C

461 ATOM 143 O GLN A 22 34.896 6.891 5.835 1.00 47.01 O

462 ATOM 144 CB GLN A 22 35.446 8.727 8.426 1.00 54.14 C

463 ATOM 145 CG GLN A 22 34.921 10.167 8.457 1.00 57.62 C

464 ATOM 146 CD GLN A 22 33.443 10.267 8.827 1.00 59.96 C

465 ATOM 147 OE1 GLN A 22 33.014 9.777 9.872 1.00 63.15 O

466 ATOM 148 NE2 GLN A 22 32.662 10.910 7.966 1.00 63.03 N

467 ATOM 149 N LEU A 23 35.423 5.551 7.566 1.00 45.76 N

468 ATOM 150 CA LEU A 23 35.926 4.501 6.696 1.00 45.96 C

469 ATOM 151 C LEU A 23 34.750 3.838 5.988 1.00 43.79 C

470 ATOM 152 O LEU A 23 34.894 3.321 4.884 1.00 43.43 O

471 ATOM 153 CB LEU A 23 36.712 3.466 7.496 1.00 46.72 C

472 ATOM 154 CG LEU A 23 38.094 3.950 7.942 1.00 48.26 C

473 ATOM 155 CD1 LEU A 23 38.787 2.868 8.758 1.00 47.77 C

474 ATOM 156 CD2 LEU A 23 38.920 4.318 6.714 1.00 46.82 C

475 ATOM 157 N SER A 24 33.585 3.857 6.631 1.00 42.94 N

476 ATOM 158 CA SER A 24 32.383 3.282 6.038 1.00 42.28 C

477 ATOM 159 C SER A 24 31.976 4.141 4.843 1.00 40.69 C

478 ATOM 160 O SER A 24 31.543 3.631 3.810 1.00 39.67 O

479 ATOM 161 CB SER A 24 31.242 3.250 7.054 1.00 44.10 C

480 ATOM 162 OG SER A 24 30.014 2.946 6.415 1.00 48.70 O

481 ATOM 163 N ASN A 25 32.112 5.451 4.991 1.00 39.26 N

482 ATOM 164 CA ASN A 25 31.778 6.353 3.904 1.00 40.49 C

483 ATOM 165 C ASN A 25 32.795 6.149 2.782 1.00 39.83 C

484 ATOM 166 O ASN A 25 32.444 6.172 1.610 1.00 37.83 O

485 ATOM 167 CB ASN A 25 31.797 7.806 4.381 1.00 42.50 C

486 ATOM 168 CG ASN A 25 30.641 8.128 5.302 1.00 45.67 C

487 ATOM 169 OD1 ASN A 25 29.493 7.797 5.009 1.00 46.05 O

488 ATOM 170 ND2 ASN A 25 30.935 8.785 6.418 1.00 47.21 N

489 ATOM 171 N ASP A 26 34.054 5.939 3.145 1.00 39.55 N

490 ATOM 172 CA ASP A 26 35.086 5.716 2.139 1.00 40.30 C

491 ATOM 173 C ASP A 26 34.869 4.390 1.410 1.00 37.74 C

492 ATOM 174 O ASP A 26 35.082 4.309 0.204 1.00 35.43 O

493 ATOM 175 CB ASP A 26 36.478 5.727 2.775 1.00 44.72 C

494 ATOM 176 CG ASP A 26 36.971 7.130 3.080 1.00 50.45 C

495 ATOM 177 OD1 ASP A 26 36.960 7.975 2.159 1.00 53.88 O

496 ATOM 178 OD2 ASP A 26 37.377 7.387 4.233 1.00 52.42 O

497 ATOM 179 N VAL A 27 34.441 3.361 2.141 1.00 35.55 N

498 ATOM 180 CA VAL A 27 34.202 2.045 1.544 1.00 36.56 C

499 ATOM 181 C VAL A 27 33.005 2.091 0.593 1.00 35.90 C

500 ATOM 182 O VAL A 27 33.039 1.514 -0.491 1.00 37.45 O

501 ATOM 183 CB VAL A 27 33.909 0.970 2.610 1.00 36.68 C

502 ATOM 184 CG1 VAL A 27 33.630 -0.358 1.927 1.00 41.01 C

503 ATOM 185 CG2 VAL A 27 35.079 0.837 3.571 1.00 39.39 C

504 ATOM 186 N ASN A 28 31.946 2.764 1.018 1.00 34.91 N

505 ATOM 187 CA ASN A 28 30.748 2.893 0.205 1.00 35.95 C

506 ATOM 188 C ASN A 28 31.104 3.580 -1.100 1.00 34.85 C

507 ATOM 189 O ASN A 28 30.644 3.174 -2.173 1.00 36.34 O

508 ATOM 190 CB ASN A 28 29.686 3.711 0.939 1.00 37.60 C

509 ATOM 191 CG ASN A 28 28.419 3.858 0.132 1.00 39.88 C

510 ATOM 192 OD1 ASN A 28 27.678 2.900 -0.041 1.00 43.47 O

511 ATOM 193 ND2 ASN A 28 28.176 5.058 -0.384 1.00 39.87 N

512 ATOM 194 N ALA A 29 31.930 4.617 -1.001 1.00 34.21 N

513 ATOM 195 CA ALA A 29 32.384 5.385 -2.154 1.00 33.85 C

514 ATOM 196 C ALA A 29 33.282 4.571 -3.088 1.00 34.90 C

515 ATOM 197 O ALA A 29 33.186 4.688 -4.308 1.00 33.29 O

516 ATOM 198 CB ALA A 29 33.123 6.634 -1.683 1.00 37.33 C

517 ATOM 199 N ALA A 30 34.152 3.744 -2.516 1.00 33.35 N

518 ATOM 200 CA ALA A 30 35.049 2.923 -3.313 1.00 33.37 C

519 ATOM 201 C ALA A 30 34.256 1.822 -4.024 1.00 32.85 C

520 ATOM 202 O ALA A 30 34.575 1.435 -5.142 1.00 32.73 O

521 ATOM 203 CB ALA A 30 36.119 2.309 -2.417 1.00 34.29 C

522 ATOM 204 N ARG A 31 33.225 1.326 -3.350 1.00 33.09 N

523 ATOM 205 CA ARG A 31 32.352 0.279 -3.874 1.00 34.88 C

524 ATOM 206 C ARG A 31 31.584 0.814 -5.077 1.00 34.81 C

525 ATOM 207 O ARG A 31 31.509 0.165 -6.121 1.00 31.90 O

526 ATOM 208 CB ARG A 31 31.377 -0.151 -2.776 1.00 38.41 C

527 ATOM 209 CG ARG A 31 30.360 -1.220 -3.163 1.00 45.28 C

528 ATOM 210 CD ARG A 31 31.023 -2.512 -3.618 1.00 49.37 C

529 ATOM 211 NE ARG A 31 30.524 -3.675 -2.888 1.00 54.07 N

530 ATOM 212 CZ ARG A 31 30.868 -3.976 -1.640 1.00 56.62 C

531 ATOM 213 NH1 ARG A 31 31.719 -3.199 -0.981 1.00 57.34 N

532 ATOM 214 NH2 ARG A 31 30.361 -5.052 -1.049 1.00 56.69 N

533 ATOM 215 N SER A 32 31.013 2.002 -4.909 1.00 33.90 N

534 ATOM 216 CA SER A 32 30.247 2.670 -5.955 1.00 35.56 C

535 ATOM 217 C SER A 32 31.120 2.996 -7.157 1.00 34.71 C

536 ATOM 218 O SER A 32 30.707 2.810 -8.301 1.00 35.10 O

537 ATOM 219 CB SER A 32 29.635 3.964 -5.411 1.00 37.93 C

538 ATOM 220 OG SER A 32 29.066 4.727 -6.464 1.00 44.88 O

539 ATOM 221 N ASP A 33 32.321 3.498 -6.886 1.00 34.12 N

540 ATOM 222 CA ASP A 33 33.277 3.851 -7.923 1.00 33.50 C

541 ATOM 223 C ASP A 33 33.671 2.628 -8.739 1.00 30.86 C

542 ATOM 224 O ASP A 33 33.718 2.685 -9.964 1.00 28.64 O

543 ATOM 225 CB ASP A 33 34.544 4.451 -7.298 1.00 37.87 C

544 ATOM 226 CG ASP A 33 34.457 5.955 -7.109 1.00 44.46 C

545 ATOM 227 OD1 ASP A 33 35.173 6.479 -6.227 1.00 47.30 O

546 ATOM 228 OD2 ASP A 33 33.690 6.612 -7.846 1.00 47.59 O

547 ATOM 229 N ALA A 34 33.983 1.535 -8.041 1.00 29.75 N

548 ATOM 230 CA ALA A 34 34.403 0.297 -8.689 1.00 28.95 C

549 ATOM 231 C ALA A 34 33.304 -0.303 -9.540 1.00 29.61 C

550 ATOM 232 O ALA A 34 33.571 -0.831 -10.609 1.00 28.52 O

551 ATOM 233 CB ALA A 34 34.866 -0.722 -7.634 1.00 28.79 C

552 ATOM 234 N GLN A 35 32.065 -0.234 -9.066 1.00 30.14 N

553 ATOM 235 CA GLN A 35 30.945 -0.783 -9.818 1.00 31.01 C

554 ATOM 236 C GLN A 35 30.721 0.025 -11.084 1.00 30.43 C

555 ATOM 237 O GLN A 35 30.402 -0.523 -12.140 1.00 30.85 O

556 ATOM 238 CB GLN A 35 29.671 -0.774 -8.957 1.00 34.91 C

557 ATOM 239 CG GLN A 35 28.410 -1.149 -9.712 1.00 41.40 C

558 ATOM 240 CD GLN A 35 28.482 -2.533 -10.322 1.00 44.71 C

559 ATOM 241 OE1 GLN A 35 28.688 -3.524 -9.621 1.00 48.25 O

560 ATOM 242 NE2 GLN A 35 28.311 -2.609 -11.638 1.00 48.49 N

561 ATOM 243 N ALA A 36 30.887 1.336 -10.970 1.00 29.99 N

562 ATOM 244 CA ALA A 36 30.714 2.240 -12.101 1.00 30.24 C

563 ATOM 245 C ALA A 36 31.797 2.009 -13.165 1.00 30.30 C

564 ATOM 246 O ALA A 36 31.531 2.117 -14.364 1.00 28.28 O

565 ATOM 247 CB ALA A 36 30.756 3.686 -11.615 1.00 30.72 C

566 ATOM 248 N ALA A 37 33.011 1.699 -12.713 1.00 29.05 N

567 ATOM 249 CA ALA A 37 34.148 1.439 -13.604 1.00 28.75 C

568 ATOM 250 C ALA A 37 33.922 0.106 -14.319 1.00 30.11 C

569 ATOM 251 O ALA A 37 34.205 -0.048 -15.511 1.00 31.18 O

570 ATOM 252 CB ALA A 37 35.425 1.368 -12.791 1.00 28.91 C

571 ATOM 253 N LYS A 38 33.420 -0.859 -13.562 1.00 31.44 N

572 ATOM 254 CA LYS A 38 33.118 -2.184 -14.093 1.00 33.07 C

573 ATOM 255 C LYS A 38 32.077 -2.074 -15.201 1.00 33.89 C

574 ATOM 256 O LYS A 38 32.221 -2.689 -16.251 1.00 31.59 O

575 ATOM 257 CB LYS A 38 32.598 -3.089 -12.970 1.00 36.11 C

576 ATOM 258 CG LYS A 38 32.088 -4.443 -13.441 1.00 39.89 C

577 ATOM 259 CD LYS A 38 31.918 -5.410 -12.281 1.00 43.43 C

578 ATOM 260 CE LYS A 38 33.261 -5.746 -11.649 1.00 46.83 C

579 ATOM 261 NZ LYS A 38 34.175 -6.451 -12.600 1.00 51.45 N

580 ATOM 262 N ASP A 39 31.026 -1.288 -14.969 1.00 34.16 N

581 ATOM 263 CA ASP A 39 29.979 -1.120 -15.972 1.00 36.44 C

582 ATOM 264 C ASP A 39 30.487 -0.361 -17.191 1.00 34.93 C

583 ATOM 265 O ASP A 39 30.101 -0.656 -18.316 1.00 35.49 O

584 ATOM 266 CB ASP A 39 28.771 -0.366 -15.402 1.00 40.22 C

585 ATOM 267 CG ASP A 39 28.091 -1.113 -14.272 1.00 44.54 C

586 ATOM 268 OD1 ASP A 39 28.036 -2.357 -14.332 1.00 45.42 O

587 ATOM 269 OD2 ASP A 39 27.601 -0.448 -13.333 1.00 48.38 O

588 ATOM 270 N ASP A 40 31.334 0.634 -16.978 1.00 32.52 N

589 ATOM 271 CA ASP A 40 31.844 1.386 -18.118 1.00 33.96 C

590 ATOM 272 C ASP A 40 32.784 0.514 -18.950 1.00 29.85 C

591 ATOM 273 O ASP A 40 32.785 0.606 -20.175 1.00 30.45 O

592 ATOM 274 CB ASP A 40 32.572 2.657 -17.670 1.00 33.83 C

593 ATOM 275 CG ASP A 40 32.507 3.757 -18.714 1.00 38.98 C

594 ATOM 276 OD1 ASP A 40 33.467 4.544 -18.820 1.00 39.61 O

595 ATOM 277 OD2 ASP A 40 31.485 3.845 -19.430 1.00 39.46 O

596 ATOM 278 N ALA A 41 33.577 -0.327 -18.289 1.00 28.33 N

597 ATOM 279 CA ALA A 41 34.505 -1.220 -18.993 1.00 29.44 C

598 ATOM 280 C ALA A 41 33.719 -2.287 -19.760 1.00 29.65 C

599 ATOM 281 O ALA A 41 34.131 -2.723 -20.838 1.00 25.38 O

600 ATOM 282 CB ALA A 41 35.487 -1.886 -17.998 1.00 28.58 C

601 ATOM 283 N ALA A 42 32.577 -2.693 -19.210 1.00 29.79 N

602 ATOM 284 CA ALA A 42 31.722 -3.679 -19.870 1.00 29.99 C

603 ATOM 285 C ALA A 42 31.124 -3.032 -21.119 1.00 29.67 C

604 ATOM 286 O ALA A 42 30.977 -3.680 -22.150 1.00 30.55 O

605 ATOM 287 CB ALA A 42 30.589 -4.134 -18.922 1.00 31.05 C

606 ATOM 288 N ARG A 43 30.766 -1.754 -21.016 1.00 29.90 N

607 ATOM 289 CA ARG A 43 30.186 -1.039 -22.149 1.00 30.25 C

608 ATOM 290 C ARG A 43 31.216 -0.941 -23.269 1.00 30.40 C

609 ATOM 291 O ARG A 43 30.903 -1.215 -24.431 1.00 29.29 O

610 ATOM 292 CB ARG A 43 29.734 0.362 -21.736 1.00 32.82 C

611 ATOM 293 CG ARG A 43 29.095 1.171 -22.861 1.00 38.97 C

612 ATOM 294 CD ARG A 43 28.414 2.435 -22.333 1.00 43.64 C

613 ATOM 295 NE ARG A 43 29.366 3.463 -21.917 1.00 46.30 N

614 ATOM 296 CZ ARG A 43 29.737 4.491 -22.674 1.00 47.66 C

615 ATOM 297 NH1 ARG A 43 29.236 4.640 -23.891 1.00 49.20 N

616 ATOM 298 NH2 ARG A 43 30.615 5.372 -22.216 1.00 49.54 N

617 ATOM 299 N ALA A 44 32.437 -0.538 -22.916 1.00 27.85 N

618 ATOM 300 CA ALA A 44 33.516 -0.424 -23.893 1.00 25.52 C

619 ATOM 301 C ALA A 44 33.687 -1.749 -24.644 1.00 25.35 C

620 ATOM 302 O ALA A 44 33.705 -1.772 -25.876 1.00 25.31 O

621 ATOM 303 CB ALA A 44 34.810 -0.040 -23.187 1.00 27.00 C

622 ATOM 304 N ASN A 45 33.802 -2.847 -23.900 1.00 25.21 N

623 ATOM 305 CA ASN A 45 33.975 -4.174 -24.488 1.00 28.03 C

624 ATOM 306 C ASN A 45 32.794 -4.676 -25.317 1.00 31.35 C

625 ATOM 307 O ASN A 45 32.978 -5.496 -26.217 1.00 31.78 O

626 ATOM 308 CB ASN A 45 34.335 -5.198 -23.401 1.00 28.51 C

627 ATOM 309 CG ASN A 45 35.805 -5.154 -23.034 1.00 29.39 C

628 ATOM 310 OD1 ASN A 45 36.666 -5.276 -23.905 1.00 27.21 O

629 ATOM 311 ND2 ASN A 45 36.105 -4.979 -21.745 1.00 27.56 N

630 ATOM 312 N GLN A 46 31.588 -4.198 -25.017 1.00 32.93 N

631 ATOM 313 CA GLN A 46 30.413 -4.590 -25.787 1.00 34.22 C

632 ATOM 314 C GLN A 46 30.409 -3.812 -27.092 1.00 34.72 C

633 ATOM 315 O GLN A 46 30.024 -4.337 -28.141 1.00 33.44 O

634 ATOM 316 CB GLN A 46 29.127 -4.298 -25.018 1.00 34.64 C

635 ATOM 317 CG GLN A 46 28.912 -5.200 -23.834 1.00 35.58 C

636 ATOM 318 CD GLN A 46 27.608 -4.911 -23.136 1.00 40.25 C

637 ATOM 319 OE1 GLN A 46 26.839 -4.057 -23.572 1.00 42.15 O

638 ATOM 320 NE2 GLN A 46 27.346 -5.623 -22.050 1.00 40.60 N

639 ATOM 321 N ARG A 47 30.824 -2.550 -27.023 1.00 33.13 N

640 ATOM 322 CA ARG A 47 30.892 -1.718 -28.216 1.00 33.01 C

641 ATOM 323 C ARG A 47 31.976 -2.285 -29.126 1.00 32.83 C

642 ATOM 324 O ARG A 47 31.872 -2.206 -30.350 1.00 36.05 O

643 ATOM 325 CB ARG A 47 31.212 -0.272 -27.844 1.00 34.84 C

644 ATOM 326 CG ARG A 47 30.115 0.414 -27.043 1.00 33.35 C

645 ATOM 327 CD ARG A 47 30.581 1.771 -26.503 1.00 33.10 C

646 ATOM 328 NE ARG A 47 30.690 2.802 -27.532 1.00 33.84 N

647 ATOM 329 CZ ARG A 47 31.206 4.006 -27.316 1.00 35.12 C

648 ATOM 330 NH1 ARG A 47 31.668 4.320 -26.110 1.00 33.52 N

649 ATOM 331 NH2 ARG A 47 31.228 4.909 -28.289 1.00 35.65 N

650 ATOM 332 N LEU A 48 33.016 -2.859 -28.528 1.00 31.40 N

651 ATOM 333 CA LEU A 48 34.084 -3.467 -29.311 1.00 33.40 C

652 ATOM 334 C LEU A 48 33.563 -4.745 -29.988 1.00 37.46 C

653 ATOM 335 O LEU A 48 33.895 -5.014 -31.138 1.00 35.92 O

654 ATOM 336 CB LEU A 48 35.303 -3.767 -28.424 1.00 30.58 C

655 ATOM 337 CG LEU A 48 36.201 -2.540 -28.166 1.00 25.20 C

656 ATOM 338 CD1 LEU A 48 37.058 -2.718 -26.928 1.00 24.86 C

657 ATOM 339 CD2 LEU A 48 37.054 -2.301 -29.389 1.00 25.54 C

658 ATOM 340 N ASP A 49 32.728 -5.515 -29.292 1.00 41.22 N

659 ATOM 341 CA ASP A 49 32.180 -6.745 -29.877 1.00 45.82 C

660 ATOM 342 C ASP A 49 31.339 -6.444 -31.122 1.00 48.43 C

661 ATOM 343 O ASP A 49 31.357 -7.204 -32.083 1.00 50.16 O

662 ATOM 344 CB ASP A 49 31.301 -7.511 -28.870 1.00 46.21 C

663 ATOM 345 CG ASP A 49 32.038 -7.878 -27.588 1.00 45.77 C

664 ATOM 346 OD1 ASP A 49 33.257 -8.140 -27.640 1.00 45.29 O

665 ATOM 347 OD2 ASP A 49 31.381 -7.920 -26.525 1.00 48.05 O

666 ATOM 348 N ASN A 50 30.600 -5.338 -31.099 1.00 51.36 N

667 ATOM 349 CA ASN A 50 29.750 -4.958 -32.228 1.00 54.22 C

668 ATOM 350 C ASN A 50 30.526 -4.365 -33.401 1.00 56.53 C

669 ATOM 351 O ASN A 50 29.926 -3.888 -34.362 1.00 57.22 O

670 ATOM 352 CB ASN A 50 28.688 -3.940 -31.793 1.00 53.30 C

671 ATOM 353 CG ASN A 50 27.768 -4.470 -30.710 1.00 54.57 C

672 ATOM 354 OD1 ASN A 50 27.692 -5.674 -30.477 1.00 52.96 O

673 ATOM 355 ND2 ASN A 50 27.049 -3.565 -30.052 1.00 53.24 N

674 ATOM 356 N MET A 51 31.852 -4.392 -33.317 1.00 59.27 N

675 ATOM 357 CA MET A 51 32.710 -3.852 -34.367 1.00 61.71 C

676 ATOM 358 C MET A 51 33.513 -4.949 -35.064 1.00 63.20 C

677 ATOM 359 O MET A 51 33.678 -4.859 -36.304 1.00 63.80 O

678 ATOM 360 CB MET A 51 33.669 -2.818 -33.775 1.00 62.63 C

679 ATOM 361 CG MET A 51 33.003 -1.543 -33.289 1.00 62.77 C

680 ATOM 362 SD MET A 51 34.125 -0.511 -32.325 1.00 64.74 S

681 ATOM 363 CE MET A 51 34.951 0.417 -33.612 1.00 64.43 C

682 TER 364 MET A 51

683 HETATM 365 O HOH A 101 34.416 5.502 -16.830 1.00 29.24 O

684 HETATM 366 O HOH A 102 30.472 7.513 0.591 1.00 49.24 O

685 HETATM 367 O HOH A 103 27.525 3.114 -25.644 1.00 56.16 O

686 HETATM 368 O HOH A 104 28.569 -2.607 -6.031 1.00 45.36 O

687 HETATM 369 O HOH A 105 27.836 2.865 -9.227 1.00 45.75 O

688 HETATM 370 O HOH A 106 33.267 8.867 2.127 1.00 50.17 O

689 HETATM 371 O HOH A 107 33.675 11.473 11.688 1.00 73.66 O

690 HETATM 372 O HOH A 108 30.240 7.202 -5.938 1.00 62.20 O

691 HETATM 373 O HOH A 109 43.925 9.173 31.092 1.00 55.68 O

692 HETATM 374 O HOH A 110 29.476 -1.870 -37.048 1.00 60.54 O

693 HETATM 375 O HOH A 111 29.249 0.902 -34.659 1.00 75.07 O

694 HETATM 376 O HOH A 112 29.495 -6.357 -38.035 1.00 57.74 O

695 HETATM 377 O HOH A 113 29.195 -6.956 -10.085 1.00 67.78 O

696 HETATM 378 O HOH A 114 34.238 8.752 -16.472 1.00 54.88 O

697 HETATM 379 O HOH A 115 27.405 -2.086 -18.861 1.00 46.59 O

698 HETATM 380 O HOH A 116 27.808 5.914 -26.134 1.00 64.75 O

699 HETATM 381 O HOH A 117 42.868 10.845 27.475 1.00 65.08 O

700 HETATM 382 O HOH A 118 33.398 6.030 24.246 1.00 62.29 O

701 HETATM 383 O HOH A 119 33.766 10.898 24.101 1.00 63.79 O

702 MASTER 273 0 0 1 0 0 0 6 382 1 0 5

703 END